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(25R)-3beta-hydroxycholest-5-en-27-oate + H2O
?
-
-
-
-
?
(glucose)4 + triacetin
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
(mannose)2 + triacetin
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
(mannose)5 + triacetin
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
(mannose)6 + triacetin
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
(xylose)2 + triacetin
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
(xylose)5 + triacetin
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
1-naphthyl acetate + H2O
naphthol + acetate
1-naphthyl butanoate + H2O
1-naphthol + butanoate
no substrate for wild-type
-
-
?
1-naphthyl caprate + H2O
1-naphthol + caprate
-
-
-
?
1-naphthyl myristate + H2O
1-naphthol + myristate
-
-
-
?
1-naphthyl octanoate + H2O
1-naphthol + octanoate
no substrate for wild-type
-
-
?
1-naphthyl propionate + H2O
1-naphthol + propionate
-
-
-
?
2 AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-2-O-acetyl-beta-D-xylopyranose + AcUXOS-3-O-acetyl-beta-D-xylopyranose + 2 acetate
2,3,4-tri-O-acetyl beta-D-xylopyranoside + H2O
4-O-acetyl beta-D-xylopyranoside + acetate
-
regioselective double deacetylation, trans arrangement of the free and acetylated OH-group at positions 2 or 3 are required for activity
-
?
2,3,4-tri-O-acetyl-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
2,4-di-O-acetyl beta-D-xylopyranoside + H2O
4-O-acetyl beta-D-xylopyranoside + acetate
-
regioselective reaction, trans arrangement of the free and acetylated OH-group at positions 2 or 3 are required for activity
-
?
2,4-di-O-acetyl-methyl beta-D-xylopyranoside + H2O
?
-
-
-
?
2-deoxy-2-fluoro-3,4-di-O-acetyl beta-D-xylopyranoside + H2O
2-deoxy-2-fluoro-4-O-acetyl beta-D-xylopyranoside + acetate
-
regioselective reaction, trans arrangement of the free and acetylated OH-group at positions 2 or 3 are required for activity
-
?
2-deoxy-3,4-di-O-acetyl beta-D-xylopyranoside + H2O
2-deoxy-4-O-acetyl beta-D-xylopyranoside + 2-deoxy-3-O-acetyl beta-D-xylopyranoside + acetate
-
regioselective reaction, trans arrangement of the free and acetylated OH-group at positions 2 or 3 are required for activity
acetylated xylopyranosides in ratio 2:1
?
2-naphthyl acetate + H2O
2-naphthol + acetate
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside + H2O
acetate + 4-nitrophenyl-beta-D-xylopyranoside
3,4-di-O-acetyl beta-D-xylopyranoside + H2O
4-O-acetyl beta-D-xylopyranoside + acetate
-
regioselective reaction, trans arrangement of the free and acetylated OH-group at positions 2 or 3 are required for activity
-
?
3,4-di-O-acetyl-methyl beta-D-xylopyranoside + H2O
?
-
-
-
?
3-deoxy-3-fluoro-2,4-di-O-acetyl beta-D-xylopyranoside + H2O
3-deoxy-3-fluoro-4-O-acetyl beta-D-xylopyranoside + acetate
-
regioselective reaction, trans arrangement of the free and acetylated OH-group at positions 2 or 3 are required for activity
-
?
3-naphthyl acetate + H2O
3-naphthol + acetate
-
-
-
-
?
4-methylumbelliferyl acetate
acetate + 4-methylumbelliferol
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl glucopyranoside + H2O
4-nitrophenol + glucose
-
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
?
4-nitrophenyl xylopyranoside + H2O
4-nitrophenol + xylose
-
-
-
-
?
4-O-methyl-D-glucuronosyl-alpha-1,2-D-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1,4-xylopyranose + H2O
4-O-methyl-D-glucuronosyl-alpha-1,2-D-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1,4-xylopyranose + beta-1,4-xylopyranosyl-beta-1,4-xylopyranose
-
-
-
-
?
4-O-methyl-glucuronoxylan + H2O
? + acetate
-
main hemicellulose in deciduous trees, and contains beta-(1,4)-linked xylopyranosyl backbone units that can be acetylated and/or substituted by alpha-(1,2)-linked 4-O-methylglucopyranosyluronic acid
-
-
?
7-amino cephalosporanic acid + H2O
? + acetate
-
-
-
-
?
7-aminocephalosporanic acid
acetate + ?
-
-
-
-
?
7-aminocephalosporanic acid + H2O
?
acetyl-xylobiose
acetate + ?
-
very low activity
-
-
?
acetylated birch-wood xylan + H2O
acetate + birch-wood xylan
acetylated birchwood xylan + H2O
acetate + birchwood xylan
-
-
-
?
acetylated birchwood xylan + H2O
deacetylated birchwood xylan + acetate
acetylated chitin + H2O
acetate + chitin
enzymatic deacetylation of chitinous substrates by AxeA is influenced by both substrate accessibility and mode of enzyme action. Barely acts on solid pure chitin whatever its form: native alpha-chitin and whiskers or native beta-chitin. But when chemically treated in strong alkali, chitin is partially deacetylated. The longer the alkali treatment, the more efficient the deacetylation of alkali-treated chitins
-
-
?
acetylated chitosan + H2O
? + acetate
acetylated colloidal chitin + H2O
? + acetate
acetylated glycol chitin + H2O
? + acetate
acetylated xylan + H2O
partially deacetylated xylan + acetate
acetylated xylan + H2O
xylan + acetate
acetylated xylooligosaccharide + H2O
?
acetylated xylooligosaccharides + H2O
?
AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-beta-D-xylopyranose + 2 acetate
AcUXOS-2-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
AcUXOS-3-O-acetyl-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + H2O
AcUXOS-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + acetate
AcUXOS-3-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
alpha-naphthyl acetate
acetate + 2-naphthol
alpha-naphthyl acetate + H2O
1-naphthol + acetate
alpha-naphthyl propionate + H2O
1-naphthol + propionate
alpha-terpinyl acetate + H2O
alpha-terpineol + acetate
-
-
-
-
?
amyl acetate
acetate + amyl alcohol
-
-
-
-
?
an acetic ester + H2O
an alcohol + acetate
aspen acetyl glucuronoxylan + H2O
?
beechwood acetyl glucuronoxylan + H2O
?
beta-D-xylose tetraacetate + H2O
?
beta-GlcNAc-(1->4)-beta-GlcNAc-(1->4)-beta-GlcNAc-(1->4)-beta-GlcNAc-(1->4)-beta-GlcNAc-(1->4)-beta-GlcNAc + H2O
?
-
native AxeA and two variants display about 50% deacetylation of the oligohexamer substrate after reaction at 50°C for 24 h in diluted culture supernatant. Characterization of the deacetylation products from reaction of wild-type and mutant AXEs, overview
-
-
?
beta-naphthyl propionate + H2O
2-naphthol + propionate
birch acetyl glucuronoxylan + H2O
?
-
positional specificity of the enzyme
-
-
?
birchwood acetyl glucuronoxylan + H2O
?
birchwood xylan + H2O
?
-
-
-
?
butyl acetate
acetate + butanol
-
-
-
-
?
cefotaxime + H2O
? + acetate
-
-
-
-
?
cellobiose octaacetate + H2O
?
-
-
-
?
cellobiose octaacetate + H2O
? + acetate
-
-
-
-
?
cellulose acetate
acetate + ?
-
-
-
-
?
cellulose acetate + H2O
?
different samples, CA0.88 is the best substrate, efficient complete degradation when the enzyme is mixed with a cellulolytic endo-1,4-beta-glucanase, EC 3.2.1.4
-
-
?
cellulose acetate + H2O
? + acetate
-
-
-
-
?
cellulose acetate + H2O
cellulose + acetate
cephalosporin C
acetate + ?
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
corncob xylan + H2O
?
-
-
-
-
?
D-galactose pentaacetate + H2O
D-galactose + acetate
low activity
-
?
D-glucose penta-acetate + H2O
?
-
deacetylation
-
-
?
D-glucose penta-acetate + H2O
? + acetate
-
-
-
-
?
D-glucose pentaacetate + H2O
?
D-glucose pentaacetate + H2O
D-glucose + acetate
-
-
-
?
D-xylose tetraacetate + H2O
?
feruloylated (3-O-Ara)2-O-acetyl-Xyl in xylooligomer + H2O
feruloylated (3-O-Ara)-Xyl in xylooligomer + acetate
-
-
-
-
?
glucose pentaacetate
acetate + ?
glucose pentaacetate + H2O
?
-
-
-
?
glucose pentaacetate + H2O
glucose + acetate
-
-
?
glucose pentacetate + H2O
?
-
-
-
-
?
hardwood acetyl glucuronoxylan
?
insoluble oat spelt xylan
?
-
-
-
?
linalyl acetate + H2O
linalool + acetate
-
-
-
-
?
methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
methyl 2,3-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 2-O-acetyl-beta-D-xylopyranoside + methyl 3-O-acetyl-beta-D-xylopyranoside
methyl 2,4-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
methyl 3,4-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
methyl beta-cellobiose + triacetin
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
methyl beta-cellobiose + vinyl acetate
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate + H2O
?
methyl beta-D-xylopyranoside 2,4-di-O-acetate + H2O
?
methyl beta-D-xylopyranoside 2-deoxy-2-fluoro-3,4-di-O-acetate + H2O
?
methyl beta-D-xylopyranoside 2-deoxy-3,4-di-O-acetate + H2O
?
methyl beta-D-xylopyranoside 3 deoxy-3-fluoro-2,4-di-O-acetate + H2O
?
methyl beta-D-xylopyranoside 3,4-di-O-acetate + H2O
?
methyl beta-D-xylopyranoside 3-deoxy-2,4-di-O-acetate + H2O
?
methyl beta-xylopyranoside + triacetin
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
methyl beta-xylopyranoside + vinyl acetate
?
-
transesterification in a microemulsion of n-hexane-vinyl acetate-sodium dioctylsulfosuccinate-water, water content of 0.4% v/v is absolutely required for activity
-
?
N,N'-diacetylchitobiose + H2O
?
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
chitobiose + acetate
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
p-nitrophenyl caprylate + H2O
p-nitrophenol + caprylate
p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitate
penta-O-acetyl-D-glucose
acetate + ?
-
-
-
-
?
sucrose octaacetate + H2O
?
-
-
-
?
tertiary-butyl acetate + H2O
tert-butanol + acetate
-
-
-
-
?
tetraacetyl-xylopyranoside + H2O
? + acetate
-
-
-
?
tri-O-acetyl-D-galactal + H2O
D-galactal + acetate
-
-
?
tri-O-acetylglycerol
acetate + ?
-
-
-
-
?
triacetin
acetate + ?
-
-
-
-
?
xylan + acetate
xylan acetate
-
-
-
-
?
xylan + H2O
?
-
deacetylation of acetylated oat spelt xylan and DMSO-extracted beechwood xylan
-
-
?
xylan acetate + H2O
xylan + acetate
-
-
-
-
r
xylose tetraacetate
acetate + ?
xylose tetraacetate + H2O
?
xylose tetraacetate + H2O
xylose + acetate
additional information
?
-
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
1-naphthyl acetate + H2O
naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
naphthol + acetate
-
-
-
-
?
2 AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-2-O-acetyl-beta-D-xylopyranose + AcUXOS-3-O-acetyl-beta-D-xylopyranose + 2 acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; preferred subunit for deacetylation by isoform CE2 and CE4
-
-
?
2 AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-2-O-acetyl-beta-D-xylopyranose + AcUXOS-3-O-acetyl-beta-D-xylopyranose + 2 acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; preferred subunit for deacetylation by isoform CE5
-
-
?
2 AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-2-O-acetyl-beta-D-xylopyranose + AcUXOS-3-O-acetyl-beta-D-xylopyranose + 2 acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; preferred subunit for deacetylation by isoform CE6
-
-
?
2 AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-2-O-acetyl-beta-D-xylopyranose + AcUXOS-3-O-acetyl-beta-D-xylopyranose + 2 acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; preferred subunit for deacetylation by isoform CE1
-
-
?
2 AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-2-O-acetyl-beta-D-xylopyranose + AcUXOS-3-O-acetyl-beta-D-xylopyranose + 2 acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; preferred subunit for deacetylation by isoform CE5
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside + H2O
acetate + 4-nitrophenyl-beta-D-xylopyranoside
-
-
-
-
?
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside + H2O
acetate + 4-nitrophenyl-beta-D-xylopyranoside
-
-
-
?
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside + H2O
acetate + 4-nitrophenyl-beta-D-xylopyranoside
-
-
-
-
?
4-methylumbelliferyl acetate
acetate + 4-methylumbelliferol
-
-
-
-
?
4-methylumbelliferyl acetate
acetate + 4-methylumbelliferol
-
-
-
-
?
4-methylumbelliferyl acetate
acetate + 4-methylumbelliferol
-
-
-
-
?
4-methylumbelliferyl acetate
acetate + 4-methylumbelliferol
-
-
-
-
?
4-methylumbelliferyl acetate
acetate + 4-methylumbelliferol
-
-
-
-
?
4-methylumbelliferyl acetate
acetate + 4-methylumbelliferol
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
?
4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylose + acetate
-
-
-
-
?
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl alpha-L-arabinose + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
DI175536
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
DI175536
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
7-aminocephalosporanic acid + H2O
?
-
-
-
-
?
7-aminocephalosporanic acid + H2O
?
-
-
-
-
?
Ac-MeGlcAXylan + H2O
?
a xylan polymer containing 4-O-methyl-D-glucopyranosyl uronic acid and acetyl groups
-
-
?
Ac-MeGlcAXylan + H2O
?
a xylan polymer containing 4-O-methyl-D-glucopyranosyl uronic acid and acetyl groups
-
-
?
acetylated birch-wood xylan + H2O
acetate + birch-wood xylan
-
5.6% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6A
-
-
?
acetylated birch-wood xylan + H2O
acetate + birch-wood xylan
-
5.8% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6B
-
-
?
acetylated birch-wood xylan + H2O
acetate + birch-wood xylan
-
5.6% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6A
-
-
?
acetylated birch-wood xylan + H2O
acetate + birch-wood xylan
-
5.8% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6B
-
-
?
acetylated birchwood xylan + H2O
deacetylated birchwood xylan + acetate
DI175536
-
-
-
?
acetylated birchwood xylan + H2O
deacetylated birchwood xylan + acetate
DI175536
-
-
-
?
acetylated chitosan + H2O
? + acetate
-
-
-
?
acetylated chitosan + H2O
? + acetate
-
-
-
?
acetylated colloidal chitin + H2O
? + acetate
-
-
-
?
acetylated colloidal chitin + H2O
? + acetate
-
-
-
?
acetylated glycol chitin + H2O
? + acetate
-
-
-
?
acetylated glycol chitin + H2O
? + acetate
-
-
-
?
acetylated xylan + H2O
?
from Eukalyptus wood
-
-
?
acetylated xylan + H2O
?
from Eukalyptus wood
-
-
?
acetylated xylan + H2O
partially deacetylated xylan + acetate
-
-
-
?
acetylated xylan + H2O
partially deacetylated xylan + acetate
-
-
-
?
acetylated xylan + H2O
xylan + acetate
-
-
-
?
acetylated xylan + H2O
xylan + acetate
acetylated xylan is the best substrate, half maximal activity with birchwood xylan
-
?
acetylated xylan + H2O
xylan + acetate
enzyme is a key component of xylan and cell wall degradation
-
?
acetylated xylan + H2O
xylan + acetate
-
substrate prepared from birchwood, the recombinant enzyme acts synergistically with xylanase to degrade acetylated xylan
-
?
acetylated xylan + H2O
xylan + acetate
the enzyme acts synergistically with xylanase to degrade acetylated xylan
-
?
acetylated xylan + H2O
xylan + acetate
-
-
-
-
?
acetylated xylan + H2O
xylan + acetate
-
-
?
acetylated xylan + H2O
xylan + acetate
acetate esters of D-xylanopyranose residues in xylan substrates
-
?
acetylated xylan + H2O
xylan + acetate
-
substrate from birchwood
-
?
acetylated xylan + H2O
xylan + acetate
-
-
-
?
acetylated xylan + H2O
xylan + acetate
catalytic mechanism, substrate with mono- and double acetylated residues, the enzyme cannot remove acetyl groups located close to large side groups such as 4-O-methylglucuronic acid
-
?
acetylated xylan + H2O
xylan + acetate
-
-
-
?
acetylated xylan + H2O
xylan + acetate
exhibits activity toward acetylated oat spelt xylan
-
-
?
acetylated xylan + H2O
xylan + acetate
exhibits activity toward acetylated oat spelt xylan
-
-
?
acetylated xylooligosaccharide + H2O
?
-
-
-
?
acetylated xylooligosaccharide + H2O
?
-
-
-
?
acetylated xylooligosaccharides + H2O
?
-
-
-
-
?
acetylated xylooligosaccharides + H2O
?
-
-
-
-
?
acetylxylan
acetate + ?
-
steamed birchwood xylan
-
-
?
acetylxylan
acetate + ?
-
-
-
-
?
acetylxylan
acetate + ?
-
-
-
-
?
acetylxylan
acetate + ?
-
birchwood acetylxylan
-
-
?
acetylxylan
acetate + ?
-
birchwood acetylxylan
-
-
?
acetylxylan
acetate + ?
-
-
-
-
?
acetylxylan
acetate + ?
-
-
-
-
?
acetylxylan
acetate + ?
-
-
-
?
acetylxylan
acetate + ?
-
larch xylan
-
-
?
acetylxylan
acetate + ?
-
larch xylan
-
-
?
acetylxylan
acetate + ?
-
-
-
-
?
acetylxylan + H2O
?
-
-
-
?
acetylxylan + H2O
?
-
-
-
?
acetylxylan + H2O
?
-
-
-
-
?
acetylxylan + H2O
?
-
-
-
-
?
acetylxylan + H2O
?
-
-
-
?
acetylxylan + H2O
?
-
-
-
?
acetylxylanacetate + ?
?
-
-
-
-
?
acetylxylanacetate + ?
?
-
-
-
-
?
AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-beta-D-xylopyranose + 2 acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-beta-D-xylopyranose + 2 acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; 2,3-di-O acetylated Xylp were nearly completely deacetylated by CE5
-
-
?
AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-beta-D-xylopyranose + 2 acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-beta-D-xylopyranose + 2 acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; 2,3-di-O acetylated Xylp were nearly completely deacetylated by CE1
-
-
?
AcUXOS-2,3-di-O-acetyl-beta-D-xylopyranose + 2 H2O
AcUXOS-beta-D-xylopyranose + 2 acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; 2,3-di-O acetylated Xylp were nearly completely deacetylated by CE5
-
-
?
AcUXOS-2-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-2-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-2-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-2-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-2-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-3-O-acetyl-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + H2O
AcUXOS-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-3-O-acetyl-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + H2O
AcUXOS-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-3-O-acetyl-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + H2O
AcUXOS-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-3-O-acetyl-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + H2O
AcUXOS-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-3-O-acetyl-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + H2O
AcUXOS-2-O-(4-methyl-alpha-D-glucopyranuronosyl)-beta-D-xylopyranose + acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-3-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; preferred subunit for deacetylation by isoform CE3
-
-
?
AcUXOS-3-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
-
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides; preferred subunit for deacetylation by isoform CE16
-
-
?
AcUXOS-3-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-3-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
AcUXOS-3-O-acetyl-beta-D-xylopyranose + H2O
AcUXOS-beta-D-xylopyranose + acetate
AcUXOS: acetylated 4-O-methyl-glucuronic acid (MeGlcA)-substituted xylo-oligosaccharides
-
-
?
alpha-naphthyl acetate
acetate + 2-naphthol
-
-
-
-
?
alpha-naphthyl acetate
acetate + 2-naphthol
-
-
-
-
?
alpha-naphthyl acetate
acetate + 2-naphthol
-
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
alpha-naphthyl propionate + H2O
1-naphthol + propionate
-
-
-
-
?
alpha-naphthyl propionate + H2O
1-naphthol + propionate
-
-
-
?
alpha-naphthyl propionate + H2O
1-naphthol + propionate
-
14.6% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6B
-
-
?
alpha-naphthyl propionate + H2O
1-naphthol + propionate
-
15.2% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6A
-
-
?
alpha-naphthyl propionate + H2O
1-naphthol + propionate
-
14.6% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6B
-
-
?
an acetic ester + H2O
an alcohol + acetate
-
-
-
-
?
an acetic ester + H2O
an alcohol + acetate
-
-
-
-
?
an acetic ester + H2O
an alcohol + acetate
-
-
-
?
an acetic ester + H2O
an alcohol + acetate
-
-
-
?
an acetic ester + H2O
an alcohol + acetate
-
-
-
?
aspen acetyl glucuronoxylan + H2O
?
-
-
-
-
?
aspen acetyl glucuronoxylan + H2O
?
-
-
-
-
?
aspen acetyl glucuronoxylan + H2O
?
-
-
-
-
?
aspen acetyl glucuronoxylan + H2O
?
-
-
-
-
?
aspen acetyl glucuronoxylan + H2O
?
-
-
-
-
?
beechwood acetyl glucuronoxylan + H2O
?
-
-
-
-
?
beechwood acetyl glucuronoxylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beta-D-xylose tetraacetate + H2O
?
-
-
-
?
beta-D-xylose tetraacetate + H2O
?
-
-
-
?
beta-D-xylose tetraacetate + H2O
?
-
-
-
?
beta-naphthyl propionate + H2O
2-naphthol + propionate
-
41.6% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6A
-
-
?
beta-naphthyl propionate + H2O
2-naphthol + propionate
-
57.3% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6B
-
-
?
birchwood acetyl glucuronoxylan + H2O
?
-
-
-
-
?
birchwood acetyl glucuronoxylan + H2O
?
-
-
-
-
?
cellulose acetate + H2O
cellulose + acetate
very low activity
-
?
cellulose acetate + H2O
cellulose + acetate
-
cleavage of acetyl at positions C2 and C3
-
?
cellulose acetate + H2O
cellulose + acetate
-
cleavage of acetyl at position C3
-
?
cellulose acetate + H2O
cellulose + acetate
-
-
-
?
cellulose acetate + H2O
cellulose + acetate
-
cleavage of acetyl at position C2
-
?
cellulose acetate + H2O
cellulose + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
deacetylation
-
-
?
D-glucose pentaacetate + H2O
?
-
10.0% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6B
-
-
?
D-glucose pentaacetate + H2O
?
-
10.3% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6A
-
-
?
D-xylose tetraacetate + H2O
?
-
10.3% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6A
-
-
?
D-xylose tetraacetate + H2O
?
-
5.0% of the activity with alpha-naphthyl acetate, acetylxylan esterase Axe6B
-
-
?
glucose pentaacetate
acetate + ?
-
glucose-beta-D-pentaacetate
-
-
?
glucose pentaacetate
acetate + ?
-
-
-
-
?
hardwood acetyl glucuronoxylan
?
-
no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s)
-
-
?
hardwood acetyl glucuronoxylan
?
-
the enzyme from Aspergillus niger is highly active compared to other acetylxylan esterases independently of the degree of polymerisation of the substrate. Mode of action, substrate specificity, and role of the family CE1 enzyme during deacetylation of soluble natural substrates, i.e. neutral and acidic O-acetylated xylooligosaccharides
-
-
?
hardwood acetyl glucuronoxylan
?
-
no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s)
-
-
?
hardwood acetyl glucuronoxylan
?
-
the target of the enzyme are 2- and 3-monoacetylated xylopyranosyl residues and also the 2,3-di-O-acetylated xylopyranosyl residues. The enzyme does not recognize as a substrate the 3-O-acetyl group on xylopyranosyl residues alpha-1,2-substituted with 4-O-methyl-D-glucuronic acid
-
-
?
hardwood acetyl glucuronoxylan
?
xylan is composed of a beta-1,4-xylosyl backbone with arabinofuranose, glucuronic acid, methylglucuronic acid and acetyl side groups. Approximately 60-70% of xylose residues in hardwood xylan are substituted with acetyl groups in the O-2 or O-3 position
-
-
?
hardwood acetyl glucuronoxylan
?
xylan is composed of a beta-1,4-xylosyl backbone with arabinofuranose, glucuronic acid, methylglucuronic acid and acetyl side groups. Approximately 60-70% of xylose residues in hardwood xylan are substituted with acetyl groups in the O-2 or O-3 position
-
-
?
hardwood acetyl glucuronoxylan
?
-
no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s)
-
-
?
hardwood acetyl glucuronoxylan
?
-
no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s)
-
-
?
hardwood acetyl glucuronoxylan
?
-
the target of the enzyme are 2- and 3-monoacetylated xylopyranosyl residues. The enzyme does not recognize as a substrate the 3-O-acetyl group on xylopyranosyl residues alpha-1,2-substituted with 4-O-methyl-D-glucuronic acid
-
-
?
hardwood acetyl glucuronoxylan
?
-
mode of action, substrate specifiicity, and role of the family CE1 enzyme during deacetylation of soluble natural substrates, i.e. neutral and acidic O-acetylated xylooligosaccharides
-
-
?
hardwood acetyl glucuronoxylan
?
-
no complete deacetylation, complete deacetylation of a hardwood acetyl glucuronoxylan requires additional deacetylating enzyme(s)
-
-
?
hardwood acetyl glucuronoxylan
?
-
the enzyme can act on di-O-acetylated Xylp residues, but may have different activities towards the O-2- and O-3-linked acetyl groups, since the content of monoacetylated Xylp units is high after enzyme action. Mode of action, substrate specifiicity, and role of the family CE5 enzyme during deacetylation of soluble natural substrates, i.e. neutral and acidic O-acetylated xylooligosac-charides, overview
-
-
?
methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
-
-
methyl 2,4-di-O-acetyl beta-D-xylopyranoside + methyl 2,3-di-O-acetyl beta-D-xylopyranoside + methyl 3,4-di-O-acetyl beta-D-xylopyranoside in the ratio 1.0:3.0:0.15
?
methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
-
-
-
?
methyl 2,3,4-tri-O-acetyl-beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
-
-
-
?
methyl 2,3-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 2-O-acetyl-beta-D-xylopyranoside + methyl 3-O-acetyl-beta-D-xylopyranoside
-
-
-
?
methyl 2,3-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 2-O-acetyl-beta-D-xylopyranoside + methyl 3-O-acetyl-beta-D-xylopyranoside
-
-
-
-
?
methyl 2,3-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 2-O-acetyl-beta-D-xylopyranoside + methyl 3-O-acetyl-beta-D-xylopyranoside
-
-
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside + methyl 2-O-acetyl-beta-D-xylopyranoside
?
methyl 2,4-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
-
-
acetate + methyl 1-O-acetyl-beta-D-xylopyranoside + methyl 4-O-acetyl-beta-D-xylopyranoside
?
methyl 2,4-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
-
-
-
?
methyl 2,4-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
-
-
-
?
methyl 3,4-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
-
-
Acetate + methyl 3-O-acetyl-beta-D-xylopyranoside + methyl 4-O-acetyl-beta-D-xylopyranoside
?
methyl 3,4-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
-
-
-
?
methyl 3,4-di-O-acetyl beta-D-xylopyranoside
acetate + methyl 4-O-acetyl-beta-D-xylopyranoside
-
-
-
?
methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate + H2O
?
-
-
-
-
?
methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate + H2O
?
-
-
-
-
?
methyl beta-D-xylopyranoside 2,4-di-O-acetate + H2O
?
-
43% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 2,4-di-O-acetate + H2O
?
-
500% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 2-deoxy-2-fluoro-3,4-di-O-acetate + H2O
?
-
180% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 2-deoxy-2-fluoro-3,4-di-O-acetate + H2O
?
-
220% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 2-deoxy-3,4-di-O-acetate + H2O
?
-
142% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 2-deoxy-3,4-di-O-acetate + H2O
?
-
38% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 3 deoxy-3-fluoro-2,4-di-O-acetate + H2O
?
-
186% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 3 deoxy-3-fluoro-2,4-di-O-acetate + H2O
?
-
650% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 3,4-di-O-acetate + H2O
?
-
322% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 3,4-di-O-acetate + H2O
?
-
170% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 3-deoxy-2,4-di-O-acetate + H2O
?
-
8% of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
methyl beta-D-xylopyranoside 3-deoxy-2,4-di-O-acetate + H2O
?
-
12 of the activity with methyl beta-D-xylopyranoside 2,3,4-tri-O-acetate
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
-
?
p-nitrophenyl caprylate + H2O
p-nitrophenol + caprylate
-
-
-
-
?
p-nitrophenyl caprylate + H2O
p-nitrophenol + caprylate
-
-
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitate
-
-
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitate
-
-
-
-
?
xanthan + H2O
?
-
bacterial polysaccharide xanthan is a polymer having a (1->4)-linked beta-D-glucopyranosyl backbone, with a beta-D-mannopyranosyl-(1->4)-beta-D-glucopyranosyluronic acid-(1->2)-alpha-D-mannopyranosyl side chain substituted to every other glucopyranosyl residue at the O-3 position. Enzyme activity towards xanthan is only observed when xanthan molecules are in the disordered conformation in complete absence of salt. The enzyme specifically removes the acetyl groups positioned on the inner mannose, acetyl groups positioned on the outer mannose are not removed at all. After a prolonged incubation at optimal conditions, 57% of all acetyl groups, representing 70% of all acetyl groups on the inner mannose units, are hydrolyzed
-
-
?
xanthan + H2O
?
-
bacterial polysaccharide xanthan is a polymer having a (1->4)-linked beta-D-glucopyranosyl backbone, with a beta-D-mannopyranosyl-(1->4)-beta-D-glucopyranosyluronic acid-(1->2)-alpha-D-mannopyranosyl side chain substituted to every other glucopyranosyl residue at the O-3 position. Enzyme activity towards xanthan is only observed when xanthan molecules are in the disordered conformation in complete absence of salt. The enzyme specifically removes the acetyl groups positioned on the inner mannose, acetyl groups positioned on the outer mannose are not removed at all. After a prolonged incubation at optimal conditions, 57% of all acetyl groups, representing 70% of all acetyl groups on the inner mannose units, are hydrolyzed
-
-
?
xylose tetraacetate
acetate + ?
-
-
-
-
?
xylose tetraacetate
acetate + ?
-
-
-
-
?
xylose tetraacetate + H2O
?
-
-
-
?
xylose tetraacetate + H2O
?
-
-
-
?
xylose tetraacetate + H2O
xylose + acetate
-
-
-
?
xylose tetraacetate + H2O
xylose + acetate
-
-
?
additional information
?
-
-
inability of CE4 AcXEs to catalyze deacetylation of 2,3-di-O-acetylated xylopyranosyl residues. Substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, mode of action of the CE4 family enzyme, overview. Regardless of the polymerization degree, each neutral oligosaccharide is converted into three forms: completely deacetylated and mono- and di-O-acetylated
-
-
?
additional information
?
-
-
isoform CE4 does not hydrolyze 4-nitrophenyl acetate
-
-
?
additional information
?
-
-
no activity towards acyl-chain substrates containing four or more carbon atoms, methyl esters of ferulic, caffeic or sinapic acids
-
-
?
additional information
?
-
-
no activity with acetylated apple pectin or acetylated sugar beet pectin
-
-
?
additional information
?
-
-
combined action of acetyl esterases and acetylxylan esterases enhances deacetylation activity
-
-
?
additional information
?
-
-
the enzyme shows partial activity with acetylated polysaccharides and neutral and acidic xylooligosaccharides, substrates are from Eucalyptus globulus xylan hydrolysate, and soluble extract of corn silage
-
-
?
additional information
?
-
no activity towards acyl-chain substrates containing four or more carbon atoms, methyl esters of ferulic, caffeic or sinapic acids
-
-
?
additional information
?
-
-
no activity towards acyl-chain substrates containing four or more carbon atoms, methyl esters of ferulic, caffeic or sinapic acids
-
-
?
additional information
?
-
-
induced by corncob powder and xylan
-
-
?
additional information
?
-
-
accessory enzyme in plant cell wall hemicellulose biodegradation pathway
-
-
?
additional information
?
-
Ser181, His298, and Asp269 form the catalytic triad, substrate binding and active site structure, overview
-
-
?
additional information
?
-
-
Ser181, His298, and Asp269 form the catalytic triad, substrate binding and active site structure, overview
-
-
?
additional information
?
-
Ser181, His298, and Asp269 form the catalytic triad, substrate binding and active site structure, overview
-
-
?
additional information
?
-
-
accessory enzyme in plant cell wall hemicellulose biodegradation pathway
-
-
?
additional information
?
-
-
induced by corncob powder and xylan
-
-
?
additional information
?
-
-
the enzyme has a double specificity on both the acetylated oligosaccharide and cephalosporin C and 7-aminocephalosporanic acid, cf. EC 3.1.1.41
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the ester linkages of the acetyl groups in both the xylose moieties of the acetylated xylan fragments
-
-
?
additional information
?
-
-
the enzyme has a double specificity on both the acetylated oligosaccharide and cephalosporin C and 7-aminocephalosporanic acid, cf. EC 3.1.1.41
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the ester linkages of the acetyl groups in both the xylose moieties of the acetylated xylan fragments
-
-
?
additional information
?
-
the enzyme shows regioselective specific activity with acetylated saccharides
-
-
?
additional information
?
-
-
the enzyme shows regioselective specific activity with acetylated saccharides
-
-
?
additional information
?
-
the enzyme shows regioselective specific activity with acetylated saccharides
-
-
?
additional information
?
-
acetyl xylan esterase Axe2 is able to hydrolyze acetyl groups both from simple acetylated xylo-oligosaccharides and complex non-soluble acetylglucuronoxylan. Axe2 has a clear preference for acetylated xylo-oligosaccharides with a high degree of substitution. For Axe2 the size of the oligomer is irrelevant. Even though there is difference in substrate affinity towards acetylated xylooligosaccharides from Eucalyptus wood, the final hydrolysis products are the same for Axe2 and Axe3: xylo-oligosaccharides containing one acetyl group located at the non-reducing xylose residue that remains, overview
-
-
?
additional information
?
-
acetyl xylan esterase Axe2 is able to hydrolyze acetyl groups both from simple acetylated xylo-oligosaccharides and complex non-soluble acetylglucuronoxylan. Axe2 has a clear preference for acetylated xylo-oligosaccharides with a high degree of substitution. For Axe2 the size of the oligomer is irrelevant. Even though there is difference in substrate affinity towards acetylated xylooligosaccharides from Eucalyptus wood, the final hydrolysis products are the same for Axe2 and Axe3: xylo-oligosaccharides containing one acetyl group located at the non-reducing xylose residue that remains, overview
-
-
?
additional information
?
-
acetyl xylan esterase Axe3 is able to hydrolyze acetyl groups both from simple acetylated xylo-oligosaccharides and complex non-soluble acetylglucuronoxylan. Axe3 shows no preference for acetylated xylo-oligosaccharides with a high degree of substitution. Axe3 has a preference for large acetylated xylo-oligosaccharides when compared to smaller acetylated xylo-oligosaccharides. Even though there is difference in substrate affinity towards acetylated xylooligosaccharides from Eucalyptus wood, the final hydrolysis products are the same for Axe2 and Axe3: xylo-oligosaccharides containing one acetyl group located at the non-reducing xylose residue that remains, overview
-
-
?
additional information
?
-
acetyl xylan esterase Axe3 is able to hydrolyze acetyl groups both from simple acetylated xylo-oligosaccharides and complex non-soluble acetylglucuronoxylan. Axe3 shows no preference for acetylated xylo-oligosaccharides with a high degree of substitution. Axe3 has a preference for large acetylated xylo-oligosaccharides when compared to smaller acetylated xylo-oligosaccharides. Even though there is difference in substrate affinity towards acetylated xylooligosaccharides from Eucalyptus wood, the final hydrolysis products are the same for Axe2 and Axe3: xylo-oligosaccharides containing one acetyl group located at the non-reducing xylose residue that remains, overview
-
-
?
additional information
?
-
acetyl xylan esterase Axe2 shows no activity with 4-nitrophenyl acetate, methyl ferulate, methyl sinapate, and methyl caffeate
-
-
?
additional information
?
-
acetyl xylan esterase Axe2 shows no activity with 4-nitrophenyl acetate, methyl ferulate, methyl sinapate, and methyl caffeate
-
-
?
additional information
?
-
acetyl xylan esterase Axe3 shows no activity with methyl ferulate, methyl sinapate, and methyl caffeate
-
-
?
additional information
?
-
acetyl xylan esterase Axe3 shows no activity with methyl ferulate, methyl sinapate, and methyl caffeate
-
-
?
additional information
?
-
acetyl xylan esterase Axe2 is able to hydrolyze acetyl groups both from simple acetylated xylo-oligosaccharides and complex non-soluble acetylglucuronoxylan. Axe2 has a clear preference for acetylated xylo-oligosaccharides with a high degree of substitution. For Axe2 the size of the oligomer is irrelevant. Even though there is difference in substrate affinity towards acetylated xylooligosaccharides from Eucalyptus wood, the final hydrolysis products are the same for Axe2 and Axe3: xylo-oligosaccharides containing one acetyl group located at the non-reducing xylose residue that remains, overview
-
-
?
additional information
?
-
acetyl xylan esterase Axe2 is able to hydrolyze acetyl groups both from simple acetylated xylo-oligosaccharides and complex non-soluble acetylglucuronoxylan. Axe2 has a clear preference for acetylated xylo-oligosaccharides with a high degree of substitution. For Axe2 the size of the oligomer is irrelevant. Even though there is difference in substrate affinity towards acetylated xylooligosaccharides from Eucalyptus wood, the final hydrolysis products are the same for Axe2 and Axe3: xylo-oligosaccharides containing one acetyl group located at the non-reducing xylose residue that remains, overview
-
-
?
additional information
?
-
acetyl xylan esterase Axe2 shows no activity with 4-nitrophenyl acetate, methyl ferulate, methyl sinapate, and methyl caffeate
-
-
?
additional information
?
-
acetyl xylan esterase Axe2 shows no activity with 4-nitrophenyl acetate, methyl ferulate, methyl sinapate, and methyl caffeate
-
-
?
additional information
?
-
acetyl xylan esterase Axe3 is able to hydrolyze acetyl groups both from simple acetylated xylo-oligosaccharides and complex non-soluble acetylglucuronoxylan. Axe3 shows no preference for acetylated xylo-oligosaccharides with a high degree of substitution. Axe3 has a preference for large acetylated xylo-oligosaccharides when compared to smaller acetylated xylo-oligosaccharides. Even though there is difference in substrate affinity towards acetylated xylooligosaccharides from Eucalyptus wood, the final hydrolysis products are the same for Axe2 and Axe3: xylo-oligosaccharides containing one acetyl group located at the non-reducing xylose residue that remains, overview
-
-
?
additional information
?
-
acetyl xylan esterase Axe3 is able to hydrolyze acetyl groups both from simple acetylated xylo-oligosaccharides and complex non-soluble acetylglucuronoxylan. Axe3 shows no preference for acetylated xylo-oligosaccharides with a high degree of substitution. Axe3 has a preference for large acetylated xylo-oligosaccharides when compared to smaller acetylated xylo-oligosaccharides. Even though there is difference in substrate affinity towards acetylated xylooligosaccharides from Eucalyptus wood, the final hydrolysis products are the same for Axe2 and Axe3: xylo-oligosaccharides containing one acetyl group located at the non-reducing xylose residue that remains, overview
-
-
?
additional information
?
-
acetyl xylan esterase Axe3 shows no activity with methyl ferulate, methyl sinapate, and methyl caffeate
-
-
?
additional information
?
-
acetyl xylan esterase Axe3 shows no activity with methyl ferulate, methyl sinapate, and methyl caffeate
-
-
?
additional information
?
-
no tributyrin hydrolyzing activity
-
-
?
additional information
?
-
-
the enzyme releases xylose from insoluble material of pretreated destarched corn bran, overview
-
-
?
additional information
?
-
-
not active with carboxymethylcellulose, larchwood xylan, ferrulic acid-arabinose-xylose polymer, p-nitrophenyl-alpha-L-arabinofuranoside, longer-chain fatty acid esters
-
-
?
additional information
?
-
-
the enzyme may play a role in enhancing hemicellulose degradation
-
-
?
additional information
?
-
-
the action of xylanase on acetylated xylan is dependent upon the initial activity of acetylxylan esterase Axe6A
-
-
?
additional information
?
-
-
not active with carboxymethylcellulose, larchwood xylan, ferrulic acid-arabinose-xylose polymer, p-nitrophenyl-alpha-L-arabinofuranoside, longer-chain fatty acid esters
-
-
?
additional information
?
-
-
the enzyme may play a role in enhancing hemicellulose degradation
-
-
?
additional information
?
-
-
the action of xylanase on acetylated xylan is dependent upon the initial activity of acetylxylan esterase Axe6A
-
-
?
additional information
?
-
wild-type protein does not show any binding activity to Avicel. The enzyme is a modular protein comprised of an esterase domain, a carbohydrate-binding module, and a region of unknown function (Fibrobacter succinogenes-specific paralogous module 1, FPm-1). The N-terminal half of Axe6B harbors the activity that cleaves side chain acetyl groups from xylan-like substrates, and the binding of insoluble xylan is determined to originate from FPm-1. Esterase activity is derived from a tetrad composed of Ser44, His273, Glu194, and Asp270, with both Glu194 and Asp270 functioning as helper acids, instead of a single carboxylate residue proposed to initiate catalysis
-
-
?
additional information
?
-
-
wild-type protein does not show any binding activity to Avicel. The enzyme is a modular protein comprised of an esterase domain, a carbohydrate-binding module, and a region of unknown function (Fibrobacter succinogenes-specific paralogous module 1, FPm-1). The N-terminal half of Axe6B harbors the activity that cleaves side chain acetyl groups from xylan-like substrates, and the binding of insoluble xylan is determined to originate from FPm-1. Esterase activity is derived from a tetrad composed of Ser44, His273, Glu194, and Asp270, with both Glu194 and Asp270 functioning as helper acids, instead of a single carboxylate residue proposed to initiate catalysis
-
-
?
additional information
?
-
-
no activity on alkyl esters longer than butanoate
-
-
?
additional information
?
-
the bifunctional acetylxylan esterase/xylanase shows xylanase and acetylxylan esterase activities on birchwood xylan
-
-
?
additional information
?
-
-
the bifunctional acetylxylan esterase/xylanase shows xylanase and acetylxylan esterase activities on birchwood xylan
-
-
?
additional information
?
-
the bifunctional acetylxylan esterase/xylanase shows xylanase and acetylxylan esterase activities on birchwood xylan
-
-
?
additional information
?
-
-
1H-NMR spectroscopy analysis of positional and substrate specificity, positional specificity of the enzyme, overview
-
-
?
additional information
?
-
-
substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, mode of action of the CE6 family enzyme, overview. On aspen glucuronoxylan hydrolysate, all neutral and acidic xylooligosaccharides present in the starting mixture are only partially deacetylated and persist in the reactionmixture mainly as mono- and di-O-acetates. The degree of acetylation is higher with shorter than longer oligosaccharides
-
-
?
additional information
?
-
-
no substrates: cellulose acetate, N-acetyl glycosamine. The enzyme shows activity towards glyceryl tributanoate and glyceryl trioleate, olive oil and fish oil
-
-
?
additional information
?
-
no substrates: 4-hydroxy-3-methoxycinnamic acid methyl ester or ethyl-4-hydroxy-3-methoxycinnamate
-
-
?
additional information
?
-
-
no substrates: 4-hydroxy-3-methoxycinnamic acid methyl ester or ethyl-4-hydroxy-3-methoxycinnamate
-
-
?
additional information
?
-
no substrates: 4-hydroxy-3-methoxycinnamic acid methyl ester or ethyl-4-hydroxy-3-methoxycinnamate
-
-
?
additional information
?
-
the enzyme Axe2 also exhibits a xylanase activity, EC 3.2.1.8. Synergistic action of the enzyme with rPcXynC on birchwood xylan, beechwood xylan and wheat arabinoxylan
-
-
?
additional information
?
-
-
the enzyme Axe2 also exhibits a xylanase activity, EC 3.2.1.8. Synergistic action of the enzyme with rPcXynC on birchwood xylan, beechwood xylan and wheat arabinoxylan
-
-
?
additional information
?
-
enzyme also exhibits a xylanase activity at an optimum pH and temperature of 5.0 and 80°C, respectively
-
-
?
additional information
?
-
the enzyme Axe2 also exhibits a xylanase activity, EC 3.2.1.8. Synergistic action of the enzyme with rPcXynC on birchwood xylan, beechwood xylan and wheat arabinoxylan
-
-
?
additional information
?
-
-
induced with triacetin
-
-
?
additional information
?
-
-
formation of monoacetates 4-, 3-, and 2-O-acetyl-methyl-beta-xylosepyranoside in a ratio 1:0.9:0.6, also of diacetates 2,3-, 3,4-, and 2,4-di-O-acetyl-methyl-beta-xylosepyranoside in a ratio 1:0.47:0.28
-
?
additional information
?
-
-
substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, overview. The enzyme converts acidic oligosaccharides mainly to mono- and di-O-acetyl derivatives, largest amount detected is mono-O-acetate is GlcAXyl8Ac, completely deacetylated MeGlcAXyl3, MeGlcAXyl4 and MeGlcAXyl5 are also observed, mode of action of the CE1 family enzyme, overview
-
-
?
additional information
?
-
-
the enzyme is able to deacetylate chitinous substrate
-
-
?
additional information
?
-
-
1H-NMR spectroscopy analysis of positional and substrate specificity, positional specificity of the enzyme, overview
-
-
?
additional information
?
-
-
inability of CE4 AcXEs to catalyze deacetylation of 2,3-di-O-acetylated xylopyranosyl residues. Substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, mode of action of the CE4 family enzyme, overview. Regardless of the polymerization degree, each neutral oligosaccharide is converted into three forms: completely deacetylated and mono- and di-O-acetylated
-
-
?
additional information
?
-
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
-
-
?
additional information
?
-
-
it is proposed that AXE I and II act in succession in xylan degradation, first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates
-
-
?
additional information
?
-
-
alpha-naphthyl acetate is a poor substrate
-
?
additional information
?
-
-
enzyme is involved in xylan degradation
-
-
?
additional information
?
-
-
the enzyme performs production of ferulic acid from lignocellulolytic agricultural biomass. Rice bran, wheat bran, bagasse and corncob are used as hydrolysis substrates for the esterase in combination with xylanase, with corncob giving the best ferulic acid yield, rice bran and bagasse are poor sources
-
-
?
additional information
?
-
-
determination of xylanase activity by measuring the release of reducing sugars from oat-spelt xylan, production of xylobiose, xylotriose and xylotetrose by a crude enzyme extract. The purified recombinant His-tagged acetylxylan esterase has broad substrate specificity for various carboxyl esters. Among the polyoxyethylenesorbate esters tested, the enzyme has the highest activity for polyoxyethylenesorbate monolaurate, but moderate or little activity for longer acyl chains. The enzyme is able to hydrolyze both acetylxylan and acetylcellulose, but acetylxylan has a better hydrolytic rate
-
-
?
additional information
?
-
-
determination of xylanase activity by measuring the release of reducing sugars from oat-spelt xylan, production of xylobiose, xylotriose and xylotetrose by a crude enzyme extract. The purified recombinant His-tagged acetylxylan esterase has broad substrate specificity for various carboxyl esters. Among the polyoxyethylenesorbate esters tested, the enzyme has the highest activity for polyoxyethylenesorbate monolaurate, but moderate or little activity for longer acyl chains. The enzyme is able to hydrolyze both acetylxylan and acetylcellulose, but acetylxylan has a better hydrolytic rate
-
-
?
additional information
?
-
-
the enzyme performs production of ferulic acid from lignocellulolytic agricultural biomass. Rice bran, wheat bran, bagasse and corncob are used as hydrolysis substrates for the esterase in combination with xylanase, with corncob giving the best ferulic acid yield, rice bran and bagasse are poor sources
-
-
?
additional information
?
-
-
combined action of acetyl esterases and acetylxylan esterases enhances deacetylation activity
-
-
?
additional information
?
-
-
the enzyme shows activity with acetylated polysaccharides and neutral and acidic xylooligosaccharides and broad specificity. Substrates are from Eucalyptus globulus xylan hydrolysate, and soluble extract of corn silage
-
-
?
additional information
?
-
-
the enzyme prefers polymeric substrates
-
-
?
additional information
?
-
-
the enzyme may play a role in enhancing hemicellulose degradation
-
-
?
additional information
?
-
-
substrate specificity together with endo-beta-1,4-xylanase of GH10 family from Clostridium thermocellum, mode of action of the CE5 family enzyme, overview. After incubation with the esterase, free and monoacetylated Xyl2, Xyl3, and Xyl4 are detected, with the free oligosaccharides predominating. The complex mixture of acetylated aldouronic acids is converted to a mixture of short free and monoacetylated MeGlcAXylx species (x = 26). The mono-acetylated species are clearly more abundant than the corresponding non-acetylated species
-
-
?
additional information
?
-
-
the enzyme acts independently of the degree of polymerisation of the substrate. Combined action of acetyl esterases and acetylxylan esterases enhances deacetylation activity
-
-
?
additional information
?
-
alpha-naphthyl acetate is a poor substrate for the enzyme and is hydrolyzed at only 1.8% of the rate observed with xylose tetraacetate. No activity is detectable on p-nitrophenyl acetate
-
-
?
additional information
?
-
-
alpha-naphthyl acetate is a poor substrate for the enzyme and is hydrolyzed at only 1.8% of the rate observed with xylose tetraacetate. No activity is detectable on p-nitrophenyl acetate
-
-
?
additional information
?
-
exhibits activity toward various chitinous substrates, but is totally inactive against 4-methylumbelliferyl acetate, beta-nitrophenyl acetate, xylose tetraacetate, and alpha-naphthyl acetate
-
-
?
additional information
?
-
-
exhibits activity toward various chitinous substrates, but is totally inactive against 4-methylumbelliferyl acetate, beta-nitrophenyl acetate, xylose tetraacetate, and alpha-naphthyl acetate
-
-
?
additional information
?
-
exhibits activity toward various chitinous substrates, but is totally inactive against 4-methylumbelliferyl acetate, beta-nitrophenyl acetate, xylose tetraacetate, and alpha-naphthyl acetate
-
-
?
additional information
?
-
alpha-naphthyl acetate is a poor substrate for the enzyme and is hydrolyzed at only 1.8% of the rate observed with xylose tetraacetate. No activity is detectable on p-nitrophenyl acetate
-
-
?
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0.0000045
-
purified enzyme, substrate 2,3,4-tri-O-acetyl beta-D-xylopyranoside
0.000056
-
purified enzyme, substrate 2-deoxy-3,4-di-O-acetyl beta-D-xylopyranoside
0.000063
-
purified enzyme, substrate 3-deoxy-2,4-di-O-acetyl beta-D-xylopyranoside
0.00016
-
purified enzyme, substrate 2-deoxy-2-fluoro-3,4-di-O-acetyl beta-D-xylopyranoside
0.0013
-
substrate xanthan, pH 5.6, 40°C
0.0016
-
purified enzyme, substrate 3-deoxy-3-fluoro-2,4-di-O-acetyl beta-D-xylopyranoside
0.02
mutant Y39P/W160S, substrate 1-naphthyl octanoate, pH 7.0, 37°C
0.03
mutant Y39G, substrate 1-naphthyl octanoate, pH 7.0, 37°C
0.034
-
purified enzyme, substrate 3,4-di-O-acetyl beta-D-xylopyranoside
0.04
mutant Y39P/W160S, substrate 1-naphthyl butanoate, pH 7.0, 37°C
0.05
mutant W160S, substrate 1-naphthyl octanoate, pH 7.0, 37°C
0.07
mutant W160A, substrate 1-naphthyl octanoate, pH 7.0, 37°C
0.08
purified recombinant enzyme, tri-O-acetyl-D-galactal
0.175
-
purified enzyme, substrate 2,4-di-O-acetyl beta-D-xylopyranoside
0.2
purified recombinant enzyme, xylose tetraacetate
0.84
mutant W160A, substrate 1-naphthyl butanoate, pH 7.0, 37°C
0.85
mutant W160S, substrate 1-naphthyl butanoate, pH 7.0, 37°C
0.87
mutant Y39G, substrate 1-naphthyl propionate, pH 7.0, 37°C
0.88
mutant Y39G/W160P, substrate 1-naphthyl propionate, pH 7.0, 37°C
1
mutant W160S, substrate 1-naphthyl acetate, pH 7.0, 37°C
1.06
-
with substrate 4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
1.4
substrate 4-nitrophenyl acetate, pH not specified in the publication, temperature not specified in the publication
1.8
mutant Y39G/W160P, substrate 1-naphthyl acetate, pH 7.0, 37°C
100.1
DI175536
substrate 4-nitrophenyl acetyte, pH 8.0, 430°C
1086
-
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-methylumbelliferyl acetate
109100
-
purified recombinant His-tagged enzyme, pH 7.5, 60°C
113
-
acetylxylan esterase Axe6A
121.5
purified recombinant enzyme, substrate acetylated xylan
1228
acetylxylan esterase activity on beta-D-xylose tetraacetate, pH 8.2, 58°C, purified recombinant enzyme
1245
-
purified recombinant enzyme, pH 7.0, 40°C, substrate glucose pentacetate
14.7
-
substrate: alpha-naphthylacetate, mutant enzyme S146A
19
-
substrate: alpha-naphthylacetate, mutant enzyme D168A
19.7
-
substrate: alpha-naphthylacetate, wild-type enzyme
2.4
-
with substrate 4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
2.72
-
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-nitrophenyl butyrate
21.9
wild-type, substrate 1-naphthyl acetate, pH 7.0, 37°C
2614
acetylxylan esterase activity on acetylxylan, pH 8.2, 58°C, purified recombinant enzyme
273.7
acetylxylan esterase activity on birchwood xylan, pH 8.2, 58°C, purified recombinant enzyme
28
substrate 2-naphthyl acetate, pH not specified in the publication, temperature not specified in the publication
2949
-
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-nitrophenyl acetate
3.9
-
substrate: alpha-naphthylpropionate, mutant enzyme S146A
31.6
-
with substrate 4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
4.8
substrate 4-nitrophenyl acetate, pH 7.0, 40°C
5
-
substrate: alpha-naphthylpropionate, wild-type D168A
55.3
-
with substrate 4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
557.9
acetylxylan esterase activity on oat spelt xylan, pH 8.2, 58°C, purified recombinant enzyme
58.6
-
acetylxylan esterase Axe6B
580.3
acetylxylan esterase activity on 4-methylumbelliferyl acetate, pH 8.2, 58°C, purified recombinant enzyme
6.6
-
substrate: alpha-naphthylpropionate, wild-type enzyme
741
-
purified recombinant enzyme, pH 7.0, 40°C, substrate alpha-naphthyl acetate
8.3
-
substrate acetylated xylooligosaccharides, pH 5.6, 40°C
80
-
purified single enzyme
873.1
acetylxylan esterase activity on beechwood xylan, pH 8.2, 58°C, purified recombinant enzyme
9.3
wild-type, substrate 1-naphthyl propionate, pH 7.0, 37°C
962
-
purified recombinant enzyme, pH 7.0, 40°C, substrate beta-naphthyl acetate
0.1
-
below, with substrate 4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
0.1
-
below, with substrate 4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
0.1
-
below, with substrate 4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
0.1
-
below, with substrate 4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
0.1
-
below, with substrate 4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
0.3
-
with substrate 4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
0.3
-
with substrate 4-nitrophenyl 3-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
0.3
-
with substrate 4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
0.31
mutant W160P, substrate 1-naphthyl butanoate, pH 7.0, 37°C
0.31
purified recombinant enzyme, glucose pentaacetate
0.49
mutant Y39P/W160S, substrate 1-naphthyl acetate, pH 7.0, 37°C
0.49
purified recombinant enzyme, 4-nitrophenyl acetate
0.5
-
with substrate 4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
0.5
-
with substrate 4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
0.59
mutant Y39G/W160P, substrate 1-naphthyl butanoate, pH 7.0, 37°C
0.59
mutant Y39P/W160S, substrate 1-naphthyl propionate, pH 7.0, 37°C
1.1
mutant W160A, substrate 1-naphthyl acetate, pH 7.0, 37°C
1.1
mutant W160P, substrate 1-naphthyl acetate, pH 7.0, 37°C
1.5
mutant W160S, substrate 1-naphthyl propionate, pH 7.0, 37°C
1.5
mutant Y39P, substrate 1-naphthyl propionate, pH 7.0, 37°C
1.6
mutant W160A, substrate 1-naphthyl propionate, pH 7.0, 37°C
1.6
mutant Y39A, substrate 1-naphthyl propionate, pH 7.0, 37°C
1.7
mutant W160P, substrate 1-naphthyl propionate, pH 7.0, 37°C
1.7
-
with substrate 4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
1.7
-
with substrate 4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
2.7
mutant Y39G, substrate 1-naphthyl acetate, pH 7.0, 37°C
2.7
-
with substrate 4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
2.7
-
with substrate 4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
3.06
-
with substrate 4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
3.06
-
with substrate 4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside, pH 5.5, 40°C
3.4
-
with substrate 4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
3.4
-
with substrate 4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
36.2
-
with substrate 4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
36.2
-
with substrate 4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside, pH 5.5, 40°C
39.86
pH 7.0, 30°C
39.86
purified recombinant enzyme, pH 7.0, 30°C
5.1
mutant Y39A, substrate 1-naphthyl acetate, pH 7.0, 37°C
5.1
mutant Y39P, substrate 1-naphthyl acetate, pH 7.0, 37°C
additional information
-
additional information
-
-
additional information
-
-
additional information
-
beta-xylosidase-coupled assay of acetylxylan esterases using monoacetylated 4-nitrophenyl beta-D-xylopyranosides
additional information
-
-
additional information
-
beta-xylosidase-coupled assay of acetylxylan esterases using monoacetylated 4-nitrophenyl beta-D-xylopyranosides
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
41.11-70.94 U/ml esterase activity in the fermentation broth of recombinant Yarrowia lipolytica strain P01g
additional information
-
-
additional information
-
-
additional information
in 50 mM Tris-HCl buffer, pH 7.0, at 60°C for 20 min: 3448 IU/micromol with acetylated xylan as substrate, 830.9 IU/micromol with glycol chitin as substrate, 306.7 IU/micromol with chitosan as substrate, 361.1 IU/micromol with colloidal chitin as substrate
additional information
-
in 50 mM Tris-HCl buffer, pH 7.0, at 60°C for 20 min: 3448 IU/micromol with acetylated xylan as substrate, 830.9 IU/micromol with glycol chitin as substrate, 306.7 IU/micromol with chitosan as substrate, 361.1 IU/micromol with colloidal chitin as substrate
additional information
-
23373 U/l/mol and 22692 U/l/mol are obtained for the wild-type and endo-H-treated enzyme forms, and 23306 U/l/mol, 23026 U/l/mol, and 22605 U/l/mol are recorded for the enzyme obtained from yeast cultures supplemented with 0.002, 0.0055 and 0.010 mg/ml tunicamycin, respectively
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Sundberg, M.; Poutanen, K.
Purification and properties of two acetylxylan esterases of Trichoderma reesei
Biotechnol. Appl. Biochem.
13
1-11
1991
Trichoderma reesei
-
brenda
Margolles-Clark, E.; Tenkanen, M.; Sderlund, H.; Penttil, M.
Acetyl xylan esterase from Trichoderma reesei contains an active-site serine residue and a cellulose-binding domain
Eur. J. Biochem.
237
553-560
1996
Trichoderma reesei
brenda
Poutanen, K.; Sundberg, M.; Korte, H.; Puls, J.
Deacetylation of xylans by acetyl esterases of Trichoderma reesei
Appl. Microbiol. Biotechnol.
33
506-510
1990
Trichoderma reesei
-
brenda
Egana, L.; Gutierrez, R.; Caputo, V.; Peirano, A.; Steiner, J.; Eyzaguirre, J.
Purification and characterization of two acetyl xylan esterases from Penicillium purpurogenum
Biotechnol. Appl. Biochem.
24
33-39
1996
Talaromyces purpureogenus
brenda
Luthi, E.; Jasmat, N.B.; Bergquist, P.L.
Overproduction of an acetylxylan esterase from extreme thermophile "Caldocellum saccharolyticum" in Escherichia coli
Appl. Microbiol. Biotechnol.
34
214-219
1990
Caldicellulosiruptor saccharolyticus
brenda
Kormelink, F.J.M.; Lefebvre, B.; Strozyk, F.; Voragen, A.G.J.
Purification and characterization of an acetyl xylan esterase from Aspergillus niger
J. Biotechnol.
27
267-282
1993
Aspergillus niger
-
brenda
Degrassi, G.; Okeke, B.C.; Bruschi, C.V.; Venturi, V.
Purification and characterization of an acetyl xylan esterase from Bacillus pumilus
Appl. Environ. Microbiol.
64
789-792
1998
Bacillus pumilus, Bacillus pumilus PS214
brenda
Bachmann, S.L.; McCarthy, A.J.
Purification and cooperative activity of enzymes constituting the xylan-degrading system of Thermomonospora fusca
Appl. Environ. Microbiol.
57
2121-2130
1991
Thermobifida fusca
brenda
Shao, W.; Wiegel, J.
Purification and characterization of two thermostable acetyl xylan esterases from Thermoanaerobacterium sp. strain JW/SL-YS485
Appl. Environ. Microbiol.
61
729-733
1995
Thermoanaerobacterium saccharolyticum, Thermoanaerobacterium saccharolyticum JW/SL-YS485
brenda
McDermid, K.P.; Forsberg, C.W.; MacKenzie, C.R.
Purification and properties of an acetylxylan esterase from Fibrobacter succinogenes S85
Appl. Environ. Microbiol.
56
3805-3810
1990
Fibrobacter succinogenes, Fibrobacter succinogenes S85
brenda
Lee, H.; To, R.J.B.; Latta, R.K.; Biely, P.; Schneider, H.
Some properties of extracellular acetylxylan esterase produced by the yeast Rhodotorula mucilaginosa
Appl. Environ. Microbiol.
53
2831-2834
1987
Rhodotorula mucilaginosa
brenda
Gutierrez, R.; Cederlund, E.; Hjelmqvist, L.; Peirano, A.; Herrera, F.; Ghosh, D.; Duax, W.; Jrnvall, H.; Eyzaguirre, J.
Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain
FEBS Lett.
423
35-38
1998
Talaromyces purpureogenus (O59893), Talaromyces purpureogenus, Trichoderma reesei
brenda
Biely, P.; Cote, G.L.; Kremnicky, L.; Greene, R.V.; Tenkanen, M.
Action of acetylxylan esterase from Trichoderma reesei on acetylated methyl glycosides
FEBS Lett.
420
121-124
1997
Trichoderma reesei
brenda
Biely, P.; Cote, G.L.; Kremnicky, L.; Greene, R.V.; Dupont, C.; Kluepfel, D.
Substrate specificity and mode of action of acetylxylan esterase from Streptomyces lividans
FEBS Lett.
396
257-260
1996
Streptomyces lividans
brenda
Hakulinen, N.; Tenkanen, M.; Rouvinen, J.
Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei
Acta Crystallogr. Sect. D
54
430-432
1998
Trichoderma reesei
brenda
Lorenz, W.W.; Wiegel, J.
Isolation, analysis, and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: a beta-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity
J. Bacteriol.
179
5436-5441
1997
Thermoanaerobacterium saccharolyticum
brenda
Biely, P.; MacKenzie, C.R.; Schneider, H.
Acetylxylan esterase of Schizophyllum commune
Methods Enzymol.
160
700-707
1988
Schizophyllum commune
-
brenda
Biely, P.; Cote, G.L.; Kremnicky, L.; Weisleder, D.; Greene, R.V.
Substrate specificity of acetylxylan esterase from Schizophyllum commune: mode of action on acetylated carbohydrates
Biochim. Biophys. Acta
1298
209-222
1996
Schizophyllum commune
brenda
Halgasova, N.; Kutejova, E.; Timko, J.
Purification and some characteristics of the acetylxylan esterase from Schizophyllum commune
Biochem. J.
298
751-755
1994
Schizophyllum commune
brenda
Christov, L.P.; Prior, B.A.
Esterases of xylan-degrading microorganisms: production, properties, and significance
Enzyme Microb. Technol.
15
460-475
1993
Aspergillus awamori, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger, Bacillus subtilis, Streptomyces sp., Fusarium oxysporum, no activity in Butyrivibrio fibrisolvens, no activity in Fibrobacter succinogenes, no activity in Neocallimastix sp., no activity in Orpinomyces sp., Rhodotorula mucilaginosa, Schizophyllum commune, Streptomyces olivochromogenes, Streptomyces flavogriseus, Thermobifida fusca, Trichoderma reesei, Streptomyces flavogriseus 45-CD, Fusarium oxysporum VTT-D-80134, Rhodotorula mucilaginosa NRC 211003, no activity in Butyrivibrio fibrisolvens NCFB 2249, no activity in Neocallimastix sp. MC-2, no activity in Fibrobacter succinogenes S85, Thermobifida fusca BS 21, Aspergillus awamori VTT-D-75028, no activity in Orpinomyces sp. PC-3
brenda
Blum, D.L.; Li, X.L.; Chen, H.; Ljungdahl, L.G.
Characterization of an acetyl xylan esterase from the anaerobic fungus Orpinomyces sp. strain PC-2
Appl. Environ. Microbiol.
65
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1999
Orpinomyces sp. (O59869)
brenda
Benini, S.; Degrassi, G.; Krastanova, I.; Lamba, D.; Venturi, V.
Purification, crystallization and preliminary X-ray analysis of an acetylxylan esterase from Bacillus pumilus
Acta Crystallogr. Sect. D
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2001
Bacillus pumilus
brenda
Kosugi, A.; Murashima, K.; Doi, R.H.
Xylanase and acetyl xylan esterase activities of XynA, a key subunit of the Clostridium cellulovorans cellulosome for xylan degradation
Appl. Environ. Microbiol.
68
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2002
Clostridium cellulovorans (Q8GH59), Clostridium cellulovorans
brenda
Cybinski, D.H.; Layton, I.; Lowry, J.B.; Dalrymple, B.P.
An acetylxylan esterase and a xylanase expressed from genes cloned from the ruminal fungus Neocallimastix patriciarum act synergistically to degrade acetylated xylans
Appl. Microbiol. Biotechnol.
52
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1999
Neocallimastix patriciarum
brenda
Biely, P.; Mastihubova, M.; Cote, G.L.; Greene, R.V.
Mode of action of acetylxylan esterase from Streptomyces lividans: a study with deoxy and deoxy-fluoro analogues of acetylated methyl beta-D-xylopyranoside
Biochim. Biophys. Acta
1622
82-88
2003
Streptomyces lividans
brenda
Biely, P.; Wong, K.K.; Suckling, I.D.; Spanikova, S.
Transacetylations to carbohydrates catalyzed by acetylxylan esterase in the presence of organic solvent
Biochim. Biophys. Acta
1623
62-71
2003
Schizophyllum commune
brenda
Chavez, R.; Schachter, K.; Navarro, C.; Peirano, A.; Bull, P.; Eyzaguirre, J.
The acetyl xylan esterase II gene from Penicillium purpurogenum is differentially expressed in several carbon sources, and tightly regulated by pH
Biol. Res.
37
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2004
Talaromyces purpureogenus (O59893), Talaromyces purpureogenus
brenda
Mukhopadhyay, A.; Hazra, P.P.; Sengupta, T.; Saha, R.; Nandi, R.; Sengupta, S.
Protein-protein interaction conferring stability to an extracellular acetyl (xylan) esterase produced by Termitomyces clypeatus
Biotechnol. Prog.
19
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2003
Termitomyces clypeatus
brenda
Harrison, M.J.; Wathugala, I.M.; Tenkanen, M.; Packer, N.H.; Nevalainen, K.M.
Glycosylation of acetylxylan esterase from Trichoderma reesei
Glycobiology
12
291-298
2002
Trichoderma reesei, Trichoderma reesei RUT C-30
brenda
Ghosh, D.; Sawicki, M.; Lala, P.; Erman, M.; Pangborn, W.; Eyzaguirre, J.; Gutierrez, R.; Jornvall, H.; Thiel, D.J.
Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 A
J. Biol. Chem.
276
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2001
Talaromyces purpureogenus (O59893), Talaromyces purpureogenus
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Altaner, C.; Saake, B.; Tenkanen, M.; Eyzaguirre, J.; Faulds, C.B.; Biely, P.; Viikari, L.; Siika-aho, M.; Puls, J.
Regioselective deacetylation of cellulose acetates by acetyl xylan esterases of different CE-families
J. Biotechnol.
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2003
Talaromyces purpureogenus, Schizophyllum commune, Streptomyces lividans, Trichoderma reesei
brenda
Hakulinen, N.; Tenkanen, M.; Rouvinen, J.
Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism
J. Struct. Biol.
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2000
Trichoderma reesei (Q99034), Trichoderma reesei
brenda
Biely, P.; Mastihubova, M.; la Grange, D.C.; van Zyl, W.H.; Prior, B.A.
Enzyme-coupled assay of acetylxylan esterases on monoacetylated 4-nitrophenyl beta-D-xylopyranosides
Anal. Biochem.
332
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2004
Schizophyllum commune, Streptomyces lividans
brenda
Krastanova, I.; Guarnaccia, C.; Zahariev, S.; Degrassi, G.; Lamba, D.
Heterologous expression, purification, crystallization, X-ray analysis and phasing of the acetyl xylan esterase from Bacillus pumilus
Biochim. Biophys. Acta
1748
222-230
2005
Bacillus pumilus, Bacillus pumilus PS213
brenda
Koseki, T.; Miwa, Y.; Fushinobu, S.; Hashizume, K.
Biochemical characterization of recombinant acetyl xylan esterase from Aspergillus awamori expressed in Pichia pastoris: mutational analysis of catalytic residues
Biochim. Biophys. Acta
1749
7-13
2005
Aspergillus awamori
brenda
Puchart, V.; Gariepy, M.C.; Shareck, F.; Dupont, C.
Identification of catalytically important amino acid residues of Streptomyces lividans acetylxylan esterase A from carbohydrate esterase family 4
Biochim. Biophys. Acta
1764
263-274
2006
Streptomyces lividans
brenda
Kam, D.K.; Jun, H.S.; Ha, J.K.; Inglis, G.D.; Forsberg, C.W.
Characteristics of adjacent family 6 acetylxylan esterases from Fibrobacter succinogenes and the interaction with the Xyn10E xylanase in hydrolysis of acetylated xylan
Can. J. Microbiol.
51
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2005
Fibrobacter succinogenes, Fibrobacter succinogenes S85
brenda
Mastihubova, M.; Biely, P.
Deoxy and deoxyfluoro analogues of acetylated methyl beta-D-xylopyranoside--substrates for acetylxylan esterases
Carbohydr. Res.
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2004
Schizophyllum commune, Trichoderma reesei
brenda
Ro, H.S.; Hong, H.P.; Kho, B.H.; Kim, S.; Chung, B.H.
Genome-wide cloning and characterization of microbial esterases
FEMS Microbiol. Lett.
233
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2004
Enterococcus faecalis (Q835Y2)
brenda
Taylor, E.J.; Gloster, T.M.; Turkenburg, J.P.; Vincent, F.; Brzozowski, A.M.; Dupont, C.; Shareck, F.; Centeno, M.S.; Prates, J.A.; Puchart, V.; Ferreira, L.M.; Fontes, C.M.; Biely, P.; Davies, G.J.
Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases
J. Biol. Chem.
281
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2006
Acetivibrio thermocellus, Streptomyces lividans
brenda
Koseki, T.; Miwa, Y.; Akao, T.; Akita, O.; Hashizume, K.
An Aspergillus oryzae acetyl xylan esterase: molecular cloning and characteristics of recombinant enzyme expressed in Pichia pastoris
J. Biotechnol.
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Aspergillus oryzae (Q75P26), Aspergillus oryzae
brenda
Martinez-Martinez, I.; Montoro-Garcia, S.; Lozada-Ramirez, J.D.; Sanchez-Ferrer, A.; Garcia-Carmona, F.
A colorimetric assay for the determination of acetyl xylan esterase or cephalosporin C acetyl esterase activities using 7-amino cephalosporanic acid, cephalosporin C, or acetylated xylan as substrate
Anal. Biochem.
369
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2007
Bacillus pumilus, Bacillus pumilus CECT 5072
brenda
Biely, P.; Mastihubova, M.; Puchart, V.
The vicinal hydroxyl group is prerequisite for metal activation of Clostridium thermocellum acetylxylan esterase
Biochim. Biophys. Acta
1770
565-570
2007
Acetivibrio thermocellus (A3DJY0), Acetivibrio thermocellus
brenda
Morley, K.L.; Chauve, G.; Kazlauskas, R.; Dupont, C.; Shareck, F.; Marchessault, R.H.
Acetyl xylan esterase-catalyzed deacetylation of chitin and chitosan
Carbohydr. Polym.
63
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2006
Streptomyces lividans (Q54413)
brenda
Ding, S.; Cao, J.; Zhou, R.; Zheng, F.
Molecular cloning, and characterization of a modular acetyl xylan esterase from the edible straw mushroom Volvariella volvacea
FEMS Microbiol. Lett.
274
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2007
Volvariella volvacea (Q09IZ4), Volvariella volvacea, Volvariella volvacea V14 (Q09IZ4)
brenda
Colombres, M.; Garate, J.A.; Lagos, C.F.; Araya-Secchi, R.; Norambuena, P.; Quiroz, S.; Larrondo, L.; Perez-Acle, T.; Eyzaguirre, J.
An eleven amino acid residue deletion expands the substrate specificity of acetyl xylan esterase II (AXE II) from Penicillium purpurogenum
J. Comput. Aided Mol. Des.
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2008
Talaromyces purpureogenus (O59893), Talaromyces purpureogenus
brenda
Gordillo, F.; Caputo, V.; Peirano, A.; Chavez, R.; Van Beeumen, J.; Vandenberghe, I.; Claeyssens, M.; Bull, P.; Ravanal, M.C.; Eyzaguirre, J.
Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene
Mycol. Res.
110
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2006
Talaromyces purpureogenus (Q8NJP6), Talaromyces purpureogenus
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Nisole, A.; Lussier, F.; Morley, K.L.; Shareck, F.; Kazlauskas, R.J.; Dupont, C.; Pelletier, J.N.
Extracellular production of Streptomyces lividans acetyl xylan esterase A in Escherichia coli for rapid detection of activity
Protein Expr. Purif.
46
274-284
2006
Streptomyces lividans
brenda
Selig, M.J.; Knoshaug, E.P.; Adney, W.S.; Himmel, M.E.; Decker, S.R.
Synergistic enhancement of cellobiohydrolase performance on pretreated corn stover by addition of xylanase and esterase activities
Bioresour. Technol.
99
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2008
Trichoderma reesei (Q99034), Trichoderma reesei, Trichoderma reesei QM9414 (Q99034)
brenda
Yang, C.; Liu, W.
Purification and properties of an acetylxylan esterase from Thermobifida fusca
Enzyme Microb. Technol.
42
181-186
2008
Thermobifida fusca, Thermobifida fusca NTU22
brenda
Liu, X.; Ding, S.
Molecular characterization of a new acetyl xylan esterase (AXEII) from edible straw mushroom Volvariella volvacea with both de-O-acetylation and de-N-acetylation activity
FEMS Microbiol. Lett.
295
50-56
2009
Volvariella volvacea (B8YIE0), Volvariella volvacea, Volvariella volvacea V14 (B8YIE0)
brenda
Yoshida, S.; Mackie, R.I.; Cann, I.K.
Biochemical and domain analyses of FSUAxe6B, a modular acetyl xylan esterase, identify a unique carbohydrate binding module in Fibrobacter succinogenes S85
J. Bacteriol.
192
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Fibrobacter succinogenes subsp. succinogenes S85 (Q9F106), Fibrobacter succinogenes subsp. succinogenes S85
brenda
Pai, C.; Wu, Z.; Chen, M.; Zeng, Y.; Chen, J.; Duan, C.; Li, M.; Liu, J.
Molecular cloning and characterization of a bifunctional xylanolytic enzyme from Neocallimastix patriciarum
Appl. Microbiol. Biotechnol.
85
1451-1462
2010
Neocallimastix patriciarum (B8YG19), Neocallimastix patriciarum, Neocallimastix patriciarum S20 (B8YG19)
brenda
Huang, Y.C.; Chen, G.H.; Chen, Y.F.; Chen, W.L.; Yang, C.H.
Heterologous expression of thermostable acetylxylan esterase gene from Thermobifida fusca and its synergistic action with xylanase for the production of xylooligosaccharides
Biochem. Biophys. Res. Commun.
400
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2010
Thermobifida fusca, Thermobifida fusca NTU22
brenda
Montoro-Garcia, S.; Gil-Ortiz, F.; Garcia-Carmona, F.; Polo, L.M.; Rubio, V.; Sanchez-Ferrer, A.
The crystal structure of the cephalosporin deacetylating enzyme acetyl xylan esterase bound to paraoxon explains the low sensitivity of this serine hydrolase to organophosphate inactivation
Biochem. J.
436
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2011
Bacillus pumilus (Q9K5F2), Bacillus pumilus, Bacillus pumilus CECT 5072 (Q9K5F2)
brenda
Huang, Y.C.; Chen, Y.F.; Chen, C.Y.; Chen, W.L.; Ciou, Y.P.; Liu, W.H.; Yang, C.H.
Production of ferulic acid from lignocellulolytic agricultural biomass by Thermobifida fusca thermostable esterase produced in Yarrowia lipolytica transformant
Biores. Technol.
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2011
Thermobifida fusca, Thermobifida fusca NTU22
brenda
Pouvreau, L.; Jonathan, M.; Kabel, M.; Hinz, S.; Gruppen, H.; Schols, H.
Characterization and mode of action of two acetyl xylan esterases from Chrysosporium lucknowense C1 active towards acetylated xylans
Enzyme Microb. Technol.
49
312-320
2011
Chrysosporium lucknowense (F2X2F9), Chrysosporium lucknowense (F2X2G0), Chrysosporium lucknowense C1 (F2X2F9), Chrysosporium lucknowense C1 (F2X2G0)
brenda
Agger, J.; Viks?-Nielsen, A.; Meyer, A.S.
Enzymatic xylose release from pretreated corn bran arabinoxylan: differential effects of deacetylation and deferuloylation on insoluble and soluble substrate fractions
J. Agric. Food Chem.
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6141-6148
2010
Favolaschia sp.
brenda
Park, S.M.
Acetyl xylan esterase of Aspergillus ficcum catalyzed the synthesis of peracetic acid from ethyl acetate and hydrogen peroxide
J. Biosci. Bioeng.
112
473-475
2011
Aspergillus ficuum
brenda
Biely, P.; Mastihubova, M.; Tenkanen, M.; Eyzaguirre, J.; Li, X.L.; Vrsanska, M.
Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of beta-D-xylopyranose and alpha-L-arabinofuranose
J. Biotechnol.
151
137-142
2011
Talaromyces purpureogenus, Schizophyllum commune, Streptomyces lividans, Trichoderma reesei
brenda
Tang, M.C.; Nisole, A.; Dupont, C.; Pelletier, J.N.; Waldron, K.C.
Chemical profiling of the deacetylase activity of acetyl xylan esterase A (AxeA) variants on chitooligosaccharides using hydrophilic interaction chromatography-mass spectrometry
J. Biotechnol.
155
257-265
2011
Streptomyces lividans
brenda
Drzewiecki, K.; Angelov, A.; Ballschmiter, M.; Tiefenbach, K.J.; Sterner, R.; Liebl, W.
Hyperthermostable acetyl xylan esterase
Microb. Biotechnol.
3
84-92
2010
Thermotoga maritima
brenda
Lansky, S.; Alalouf, O.; Solomon, V.; Alhassid, A.; Govada, L.; Chayen, N.E.; Chayan, N.E.; Belrhali, H.; Shoham, Y.; Shoham, G.
Crystallization and preliminary crystallographic analysis of Axe2, an acetylxylan esterase from Geobacillus stearothermophilus
Acta Crystallogr. Sect. F
69
430-434
2013
Geobacillus stearothermophilus (Q09LX1), Geobacillus stearothermophilus, Geobacillus stearothermophilus T-6 (Q09LX1)
brenda
Lansky, S.; Alalouf, O.; Salama, R.; Dvir, H.; Shoham, Y.; Shoham, G.
Preliminary crystallographic analysis of a double mutant of the acetyl xylo-oligosaccharide esterase Axe2 in its dimeric form
Acta Crystallogr. Sect. F
70
476-481
2014
Geobacillus stearothermophilus (Q09LX1), Geobacillus stearothermophilus T-6 (Q09LX1)
brenda
Waters, D.M.; Murray, P.G.; Miki, Y.; Martinez, A.T.; Tuohy, M.G.; Faulds, C.B.
Cloning, overexpression in Escherichia coli, and characterization of a thermostable fungal acetylxylan esterase from Talaromyces emersonii
Appl. Environ. Microbiol.
78
3759-3762
2012
Rasamsonia emersonii (E9M3D1), Rasamsonia emersonii, Rasamsonia emersonii IMI 392299 (E9M3D1)
brenda
Tian, Q.; Song, P.; Jiang, L.; Li, S.; Huang, H.
A novel cephalosporin deacetylating acetyl xylan esterase from Bacillus subtilis with high activity toward cephalosporin C and 7-aminocephalosporanic acid
Appl. Microbiol. Biotechnol.
98
2081-2089
2014
Bacillus subtilis, Bacillus subtilis CICC 20034
brenda
Uhliarikova, I.; Vrsanska, M.; McCleary, B.V.; Biely, P.
Positional specificity of acetylxylan esterases on natural polysaccharide: an NMR study
Biochim. Biophys. Acta
1830
3365-3372
2013
Orpinomyces sp., Streptomyces lividans
brenda
Biely, P.; Cziszarova, M.; Uhliarikova, I.; Agger, J.W.; Li, X.L.; Eijsink, V.G.; Westereng, B.
Mode of action of acetylxylan esterases on acetyl glucuronoxylan and acetylated oligosaccharides generated by a GH10 endoxylanase
Biochim. Biophys. Acta
1830
5075-5086
2013
Acetivibrio thermocellus, Orpinomyces sp., Schizophyllum commune, Streptomyces lividans, Trichoderma reesei
brenda
Neumueller, K.G.; Streekstra, H.; Gruppen, H.; Schols, H.A.
Trichoderma longibrachiatum acetyl xylan esterase 1 enhances hemicellulolytic preparations to degrade corn silage polysaccharides
Biores. Technol.
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2014
Aspergillus niger, Trichoderma longibrachiatum
brenda
Moriyoshi, K.; Koma, D.; Yamanaka, H.; Sakai, K.; Ohmoto, T.
Expression and characterization of a thermostable acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis involved in the degradation of insoluble cellulose acetate
Biosci. Biotechnol. Biochem.
77
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2013
Caldanaerobacter subterraneus (Q8RBF4), Caldanaerobacter subterraneus, Caldanaerobacter subterraneus DSM 15242 (Q8RBF4)
brenda
Kool, M.M.; Schols, H.A.; Wagenknecht, M.; Hinz, S.W.; Moerschbacher, B.M.; Gruppen, H.
Characterization of an acetyl esterase from Myceliophthora thermophila C1 able to deacetylate xanthan
Carbohydr. Polym.
111
222-229
2014
Thermothelomyces thermophilus, Thermothelomyces thermophilus C1
brenda
Huy, N.D.; Thiyagarajan, S.; Kim, D.H.; Park, S.M.
Cloning and characterization of a novel bifunctional acetyl xylan esterase with carbohydrate binding module from Phanerochaete chrysosporium
J. Biosci. Bioeng.
115
507-513
2013
Phanerodontia chrysosporium (H2ESB9), Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767 (H2ESB9)
brenda
Koutaniemi, S.; van Gool, M.P.; Juvonen, M.; Jokela, J.; Hinz, S.W.; Schols, H.A.; Tenkanen, M.
Distinct roles of carbohydrate esterase family CE16 acetyl esterases and polymer-acting acetyl xylan esterases in xylan deacetylation
J. Biotechnol.
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684-692
2013
Aspergillus niger, Trichoderma reesei, Thermothelomyces thermophilus
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Tian, B.; Chen, Y.; Ding, S.
A combined approach for improving alkaline acetyl xylan esterase production in Pichia pastoris, and effects of glycosylation on enzyme secretion, activity and stability
Protein Expr. Purif.
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2012
Volvariella volvacea
brenda
Till, M.; Goldstone, D.C.; Attwood, G.T.; Moon, C.D.; Kelly, W.J.; Arcus, V.L.
Structure and function of an acetyl xylan esterase (Est2A) from the rumen bacterium Butyrivibrio proteoclasticus
Proteins
81
911-917
2013
Butyrivibrio proteoclasticus (E0RVY7), Butyrivibrio proteoclasticus, Butyrivibrio proteoclasticus B316 (E0RVY7)
brenda
Juturu, V.; Aust, C.; Wu, J.C.
Heterologous expression and biochemical characterization of acetyl xylan esterase from Coprinopsis cinerea
World J. Microbiol. Biotechnol.
29
597-605
2013
Coprinopsis cinerea (Q09IZ4), Coprinopsis cinerea, Coprinopsis cinerea Okayama 7 (Q09IZ4), Coprinopsis cinerea Okayama 7
brenda
Waters, D.M.; Murray, P.G.; Miki, Y.; Martinez, A.T.; Tuohy, M.G.; Faulds, C.B.
Cloning, overexpression in Escherichia coli, and characterization of a thermostable fungal acetylxylan esterase from Talaromyces emersonii
Appl. Environ. Microbiol.
78
3759-3762
2012
Rasamsonia emersonii (E9M3D1), Rasamsonia emersonii
brenda
Huy, N.D.; Thayumanavan, P.; Kwon, T.H.; Park, S.M.
Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium
J. Biosci. Bioeng.
116
152-159
2013
Phanerodontia chrysosporium (H2ESB9)
brenda
Komiya, D.; Hori, A.; Ishida, T.; Igarashi, K.; Samejima, M.; Koseki, T.; Fushinobu, S.
Crystal structure and substrate specificity modification of acetyl xylan esterase from Aspergillus luchuensis
Appl. Environ. Microbiol.
83
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Aspergillus luchuensis (Q92194), Aspergillus luchuensis
brenda
Kwon, M.; Song, J.; Park, H.; Park, H.; Chang, J.
Characterization of heterologously expressed acetyl xylan esterase1 isolated from the anaerobic rumen fungus Neocallimastix frontalis PMA02
Asian-Australas. J. Anim. Sci.
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1576-1584
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Neocallimastix frontalis (DI175536), Neocallimastix frontalis PMA02 (DI175536)
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Mai-Gisondi, G.; Maaheimo, H.; Chong, S.; Hinz, S.; Tenkanen, M.; Master, E.
Functional comparison of versatile carbohydrate esterases from families CE1, CE6 and CE16 on acetyl-4-O-methylglucuronoxylan and acetyl-galactoglucomannan
Biochim. Biophys. Acta
1861
2398-2405
2017
Aspergillus nidulans
brenda
Razeq, F.; Jurak, E.; Stogios, P.; Yan, R.; Tenkanen, M.; Kabel, M.; Wang, W.; Master, E.
A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans
Biotechnol. Biofuels
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74
2018
Flavobacterium johnsoniae
brenda
Neumueller, K.; De Souza, A.; Van Rijn, J.; Streekstra, H.; Gruppen, H.; Schols, H.
Positional preferences of acetyl esterases from different CE families towards acetylated 4-O-methyl glucuronic acid-substituted xylo-oligosaccharides
Biotechnol. Biofuels
8
7-7
2015
Aspergillus niger, Acetivibrio thermocellus, Rasamsonia emersonii (E9M3D1), Orpinomyces sp. PC-2 (O59869), Trichoderma reesei (Q99034)
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Liu, S.; Ding, S.
Replacement of carbohydrate binding modules improves acetyl xylan esterase activity and its synergistic hydrolysis of different substrates with xylanase
BMC Biotechnol.
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Volvariella volvacea (Q09IZ4)
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Wang, Y.; Sakka, M.; Yagi, H.; Kaneko, S.; Katsuzaki, H.; Kunitake, E.; Kimura, T.; Sakka, K.
Ruminiclostridium josui Abf62A-Axe6A A tri-functional xylanolytic enzyme exhibiting alpha-l-arabinofuranosidase, endoxylanase, and acetylxylan esterase activities
Enzyme Microb. Technol.
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Ruminiclostridium josui (WP_024831741), Ruminiclostridium josui, Ruminiclostridium josui JCM 1788 (WP_024831741)
brenda
Adesioye, F.A.; Makhalanyane, T.P.; Biely, P.; Cowan, D.A.
Phylogeny, classification and metagenomic bioprospecting of microbial acetyl xylan esterases
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uncultured microorganism
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Shahid, S.; Tajwar, R.; Akhtar, M.W.
A novel trifunctional, family GH10 enzyme from Acidothermus cellulolyticus 11B, exhibiting endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities
Extremophiles
22
109-119
2018
Acidothermus cellulolyticus (A0LR95), Acidothermus cellulolyticus 11B (A0LR95), Acidothermus cellulolyticus 11B
brenda
Yang, Y.; Zhu, N.; Yang, J.; Lin, Y.; Liu, J.; Wang, R.; Wang, F.; Yuan, H.
A novel bifunctional acetyl xylan esterase/arabinofuranosidase from Penicillium chrysogenum P33 enhances enzymatic hydrolysis of lignocellulose
Microb. Cell Fact.
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166
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Penicillium chrysogenum (A0A2H4V677), Penicillium chrysogenum, Penicillium chrysogenum P33 (A0A2H4V677)
brenda
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Expression of fungal acetyl xylan esterase in Arabidopsis thaliana improves saccharification of stem lignocellulose
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Aspergillus niger (A2QZI3), Aspergillus niger, Aspergillus niger FGSC A1513 (A2QZI3)
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Park, S.; Yoo, W.; Lee, C.; Jeong, C.; Shin, S.; Kim, H.; Park, H.; Kim, K.; Kim, T.; Lee, J.
Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.
PLoS ONE
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Paenibacillus sp. R4
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Manavalan, T.; Liu, R.; Zhou, Z.; Zou, G.
Optimization of acetyl xylan esterase gene expression in Trichoderma reesei and its application to improve the saccharification efficiency on different biomasses
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Aspergillus oryzae, Aspergillus oryzae NBRC 100959
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Eminoglu, A.; Uelker, S.; Sandalli, C.
Cloning, purification and characterization of acetyl xylane esterase from Anoxybacillus flavithermus DSM 2641(T) with activity on low molecular-weight acetates
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Anoxybacillus flavithermus, Anoxybacillus flavithermus DSM 2641(T)
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