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3-amino-3-phenylpropionic acid ethyl ester + H2O
?
-
-
-
-
?
4-carbamimidamidobenzyl L-isoleucinate + H2O
L-isoleucine + 1-[4-(hydroxymethyl)phenyl]guanidine
-
-
-
-
?
4-carbamimidamidobenzyl L-phenylalaninate + H2O
L-phenylalanine + 1-[4-(hydroxymethyl)phenyl]guanidine
-
-
-
-
?
4-carbamimidamidobenzyl L-valinate + H2O
L-valine + 1-[4-(hydroxymethyl)phenyl]guanidine
-
-
-
-
?
4-hydroxy-D-phenylglycine methyl ester + H2O
4-hydroxy-D-phenylglycine + methanol
5'-O-L-valyl-2'-deoxy-5-fluorouridine + H2O
L-valine + 2'-deoxy-5-fluorouridine
-
-
-
-
?
acetyl-D-phenyl methyl ester + L-leucine amide
acetyl-D-phenyl-L-leucine + methanol
-
-
-
?
acetyl-D-phenyl methyl ester + L-phenylalanine amide
acetyl-D-phenyl-L-phenylalanine + methanol
-
-
-
?
acetyl-D-phenylalanine methyl ester + H2O
acetyl-D-phenylalanine + methanol
-
-
-
r
acetyl-L-phenylalanine methyl ester + H2O
acetyl-L-phenylalanine + methanol
-
-
-
r
alpha-aminoisobutyric acid methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
alpha-aminoisobutyric acid methyl ester + H2O
alpha-aminoisobutyric acid + methanol
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
beta-Ala benzyl ester + H2O
beta-Ala + benzoic acid
-
-
-
-
?
beta-alanyl methyl ester + L-tryptophan
beta-alanyl-L-tryptophan + methanol
about 100% of the activity with L-isoleucyl methyl ester
-
-
?
cefatrizine + H2O
?
-
-
-
-
?
cefradine + H2O
?
Pseudomonas melanogenum
-
hydrolysis
-
-
?
cephalexin + H2O
7-amino-3-deacetoxycephalosporanic acid + phenylglycine
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
cephaloglycin + H2O
?
-
-
-
-
?
D-2-nitro-5-[(phenylglycyl)amino]benzoic acid + H2O
?
-
-
-
?
D-2-nitro-5-[(phenylglycyl)amino]benzoic acid + H2O
phenylglycine + p-nitrophenol
-
-
r
D-4-hydroxyphenylglycine methyl ester + H2O
D-4-hydroxyphenylglycine + methanol
-
-
-
-
?
D-alanine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
D-alanine methyl ester + H2O
D-alanine + methanol
D-alpha-phenylglycine ethyl ester + 7-amino-3-deacetoxycephalosporanic acid
ethanol + cephalexin
-
-
-
?
D-alpha-phenylglycine ethyl ester + H2O
D-alpha-phenylglycine + ethanol
-
-
-
?
D-alpha-phenylglycine isopropyl ester + 7-amino-3-deacetoxycephalosporanic acid
isopropanol + cephalexin
-
-
-
?
D-alpha-phenylglycine isopropyl ester + H2O
D-alpha-phenylglycine + isopropanol
-
-
-
?
D-alpha-phenylglycine methyl ester + 6-aminopenicillanic acid
methanol + ?
-
-
-
?
D-alpha-phenylglycine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + cephalexin
D-alpha-phenylglycine methyl ester + 7-aminocephalosporanic acid
methanol + ?
D-alpha-phenylglycine methyl ester + H2O
D-alpha-phenylglycine + methanol
D-alpha-phenylglycine n-butyl ester + 7-amino-3-deacetoxycephalosporanic acid
butanol + cephalexin
-
-
-
?
D-alpha-phenylglycine n-butyl ester + H2O
D-alpha-phenylglycine + n-butanol
-
-
-
?
D-alpha-phenylglycine n-propyl ester + 7-amino-3-deacetoxycephalosporanic acid
n-propanol + cephalexin
-
-
-
?
D-alpha-phenylglycine n-propyl ester + H2O
D-alpha-phenylglycine + n-propanol
-
-
-
?
D-aspartate dimethyl ester + H2O
D-aspartate + methanol
-
-
-
r
D-leucine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
D-leucine methyl ester + H2O
D-leucine + methanol
-
-
-
?
D-methionine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
D-methionine methyl ester + H2O
D-methionine + methanol
D-phenylalanine amide + H2O
D-phenylalanine + NH3
-
-
-
?
D-phenylalanine methyl ester + H2O
D-phenylalanine + methanol
-
-
-
r
D-phenylglycine amide + H2O
D-phenylglycine + NH3
D-phenylglycine methyl ester + 6-amino penicillanic acid
ampicillin
-
specific for D-isomer
-
?
D-phenylglycine methyl ester + 7-amino-desacetoxycephalosporanic acid
cephalexin + H2O
-
-
-
r
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
D-serine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
D-serine methyl ester + H2O
D-serine + methanol
-
-
-
?
D-tryptophan methyl ester + H2O
D-tryptophan + methanol
-
-
-
r
D-tyrosine methyl ester + H2O
D-tyrosine + methanol
-
-
-
r
DL-alpha-aminobutyric acid methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
DL-alpha-aminobutyric acid methyl ester + H2O
DL-alpha-aminobutyric acid + methanol
-
-
-
?
DL-phenylglycine methyl ester + 6-amino penicillanic acid
ampicillin
-
more than 85% of D-phenylglycine methyl ester is transformed into ampicillin
-
?
DL-threonine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
DL-threonine methyl ester + H2O
DL-threonine + methanol
-
-
-
?
ethyl DL-alpha-amino-n-butyrate + H2O
?
-
-
-
-
?
floxuridine + H2O
?
-
-
-
-
?
gemcitabine + H2O
?
-
-
-
-
?
Gly benzyl ester + H2O
Gly + benzoic acid
-
-
-
-
?
glycine ethyl ester + 7-aminocephalosporanic acid
ethanol + ?
-
-
-
?
glycine ethyl ester + H2O
glycine + ethanol
-
-
-
?
glycine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
glycine methyl ester + H2O
glycine + methanol
-
-
-
?
glycyl methyl ester + L-tryptophan
glycyl-L-tryptophan + methanol
about 230% of the activity with L-isoleucyl methyl ester
-
-
?
L-Ala benzyl ester + H2O
L-Ala + benzoic acid
-
-
-
-
?
L-alanyl methyl ester + L-tryptophan
L-alanyl-L-tryptophan + methanol
about 240% of the activity with L-isoleucyl methyl ester
-
-
?
L-alpha-phenylglycine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + cephalexin
-
-
-
?
L-arginine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
L-arginine methyl ester + H2O
L-arginine + methanol
-
-
-
?
L-arginyl methyl ester + L-tryptophan
L-arginyl-L-tryptophan + methanol
about 220% of the activity with L-isoleucyl methyl ester
-
-
?
L-aspartate dimethyl ester + H2O
L-aspartate + methanol
-
-
-
?
L-aspartyl methyl ester + L-tryptophan
L-aspartyl-L-tryptophan + methanol
about 200% of the activity with L-isoleucyl methyl ester
-
-
?
L-cysteine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
L-cysteine methyl ester + H2O
L-cysteine + methanol
L-glutamic acid methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
L-glutamic acid methyl ester + H2O
L-glutamic acid + methanol
-
-
-
?
L-isoleucyl methyl ester + L-tryptophan
L-isoleucyl-L-tryptophan + methanol
-
-
-
?
L-Leu benzyl ester + H2O
L-leu + benzoic acid
-
-
-
-
?
L-leucine ethyl ester + H2O
L-leucine + ethanol
-
-
-
?
L-lysine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
L-lysine methyl ester + H2O
L-lysine + methanol
-
-
-
?
L-Met methyl ester + H2O
?
-
-
-
-
?
L-methionine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
L-methionine methyl ester + H2O
L-methionine + methanol
L-Phe benzyl ester + H2O
L-Phe + benzoic acid
-
-
-
-
?
L-Phe ethyl ester + H2O
?
-
-
-
-
?
L-phenylalanine ethyl ester + H2O
L-phenylalanine + ethanol
-
-
-
?
L-phenylalanine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
L-phenylalanine methyl ester + H2O
L-phenylalanine + methanol
L-Pro benzyl ester + H2O
L-Pro + benzoic acid
-
-
-
-
?
L-proyl methyl ester + L-tryptophan
L-prolyl-L-tryptophan + methanol
about 240% of the activity with L-isoleucyl methyl ester
-
-
?
L-Ser benzyl ester + H2O
L-Ser + benzoic acid
-
-
-
-
?
L-serine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
L-serine methyl ester + H2O
L-serine + methanol
L-Trp benzyl ester + H2O
L-Trp + benzoic acid
-
-
-
-
?
L-tryptophan methyl ester + H2O
L-tryptophan + methanol
-
-
-
r
L-tryptophanyl methyl ester + L-tryptophan
L-tryptophanyl-L-tryptophan + methanol
-
-
-
?
L-Tyr benzyl ester + H2O
L-Tyr + benzoic acid
-
-
-
-
?
L-tyrosine ethyl ester + H2O
L-tyrosine + ethanol
-
-
-
?
L-tyrosine methyl ester + H2O
L-tyrosine + methanol
-
-
-
r
L-tyrosine propyl ester + H2O
L-tyrosine + propanol
-
-
-
?
L-Val benzyl ester + H2O
L-Val + benzoic acid
-
-
-
-
?
L-valine methyl ester + H2O
L-valine + methanol
-
-
-
-
?
methyl acetate
acetate + methanol
-
1.1% of activity with D-phenylalanine methylester
-
?
methyl butyrate
butyrate + methanol
-
3.6% of activity with D-phenylalanine methylester
-
?
methyl caproate
caproate + methanol
-
2% of activity with D-phenylalanine methylester
-
?
methyl caprylate
caprylate + methanol
-
1.1% of activity with D-phenylalanine methylester
-
?
methyl propionate
propionate + methanol
-
2.7% of activity with D-phenylalanine methylester
-
?
p-hydroxyphenylpropionic acid ethyl ester + H2O
p-hydroxyphenylpropionic acid + ethanol
-
-
-
?
p-nitrophenyl-p'-guanidino benzoate + H2O
p-guanidino benzoate + p-nitrophenol
-
-
-
?
phenylalanine benzyl ester + H2O
L-phenylalanine + benzyl alcohol
-
-
-
-
?
phenylalanine ethyl ester + H2O
L-phenylalanine + ethanol
-
-
-
-
?
phenylalanine methyl ester + H2O
L-phenylalanine + methanol
-
-
-
-
?
phenylalanine [3-(hydroxymethyl)phenyl]guanidine + H2O
L-phenylalanine + [3-(hydroxymethyl)phenyl]guanidine
-
-
-
-
?
S-benzyl-L-cysteine ethyl ester + H2O
S-benzyl-L-cysteine + ethanol
-
-
-
-
?
valacyclovir + H2O
L-valine + 2-amino-9-[(2-hydroxyethyloxy)methyl]-1,9-dihydro-6H-purin-6-one
-
-
-
-
?
valacyclovir + H2O
L-valine + acyclovir
-
-
-
-
?
valganciclovir + H2O
?
-
-
-
-
?
valganciclovir + H2O
L-valine + 2-amino-9-[[(1,3-dihydroxpropan-2-yl)oxy]methyl]-1,9-dihydro-6H-purin-6-one
-
-
-
-
?
valganciclovir + H2O
L-valine + ganciclovir
-
-
-
-
?
valine 4-nitrobenzyl ester + H2O
L-valine + 4-nitrobenzyl alcohol
-
-
-
-
?
valine benzyl ester + H2O
L-valine + benzyl alcohol
-
-
-
-
?
valine [3-(aminomethyl)phenyl]guanidine + H2O
L-valine + [3-(aminomethyl)phenyl]guanidine
-
-
-
-
?
valine [3-(hydroxymethyl)phenyl]guanidine + H2O
L-valine + [3-(hydroxymethyl)phenyl]guanidine
-
-
-
-
?
zidovudine + H2O
?
-
-
-
-
?
additional information
?
-
4-hydroxy-D-phenylglycine methyl ester + H2O
4-hydroxy-D-phenylglycine + methanol
-
-
-
-
?
4-hydroxy-D-phenylglycine methyl ester + H2O
4-hydroxy-D-phenylglycine + methanol
-
-
-
?
4-hydroxy-D-phenylglycine methyl ester + H2O
4-hydroxy-D-phenylglycine + methanol
-
-
-
-
?
alpha-aminoisobutyric acid methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
alpha-aminoisobutyric acid methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
alpha-aminoisobutyric acid methyl ester + H2O
alpha-aminoisobutyric acid + methanol
-
-
-
?
alpha-aminoisobutyric acid methyl ester + H2O
alpha-aminoisobutyric acid + methanol
-
-
-
?
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
-
-
?
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
?
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
-
?
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
-
-
?
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
r
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
the enzyme catalyzes ampicillin synthesis and hydrolysis
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
the enzyme catalyzes ampicillin synthesis and hydrolysis
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
Pseudomonas melanogenum
-
the enzyme catalyzes ampicillin synthesis and hydrolysis
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
Pseudomonas melanogenum ATCC 17808
-
the enzyme catalyzes ampicillin synthesis and hydrolysis
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
Pseudomonas melanogenum IFO 12020
-
the enzyme catalyzes ampicillin synthesis and hydrolysis
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
Pseudomonas melanogenum KY3987
-
the enzyme catalyzes ampicillin synthesis and hydrolysis
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
Pseudomonas melanogenum KY8540
-
the enzyme catalyzes ampicillin synthesis and hydrolysis
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
binding structure, modeling
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
binding structure, modeling
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
-
?
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
-
-
-
?
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
-
-
-
?
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
-
-
-
?
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
-
-
-
r
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
-
-
-
r
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
-
-
-
r
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
-
-
r
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
-
-
-
?, r
an alpha-aminoacid ester + H2O
an alpha-amino acid + an alcohol
-
-
-
?, r
cefadroxil + H2O
?
-
-
-
-
?
cefadroxil + H2O
?
-
-
-
-
?
cefadroxil + H2O
?
-
-
-
-
?
cefaloglycin + H2O
?
-
-
-
-
?
cefaloglycin + H2O
?
Pseudomonas melanogenum
-
hydrolysis
-
-
?
cephalexin + H2O
7-amino-3-deacetoxycephalosporanic acid + phenylglycine
-
-
-
r
cephalexin + H2O
7-amino-3-deacetoxycephalosporanic acid + phenylglycine
-
-
-
-
r
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
r
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
r
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
Pseudomonas melanogenum
-
the enzyme catalyzes cephalexin synthesis and hydrolysis
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
Pseudomonas melanogenum ATCC 17808
-
the enzyme catalyzes cephalexin synthesis and hydrolysis
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
Pseudomonas melanogenum IFO 12020
-
the enzyme catalyzes cephalexin synthesis and hydrolysis
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
Pseudomonas melanogenum KY3987
-
the enzyme catalyzes cephalexin synthesis and hydrolysis
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
Pseudomonas melanogenum KY8540
-
the enzyme catalyzes cephalexin synthesis and hydrolysis
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
?
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
?
D-alanine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
D-alanine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
D-alanine methyl ester + H2O
D-alanine + methanol
-
-
-
?
D-alanine methyl ester + H2O
D-alanine + methanol
-
-
-
?
D-alpha-phenylglycine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + cephalexin
-
-
-
r
D-alpha-phenylglycine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + cephalexin
-
-
-
?
D-alpha-phenylglycine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + cephalexin
-
-
-
?
D-alpha-phenylglycine methyl ester + 7-aminocephalosporanic acid
methanol + ?
-
-
-
-
?
D-alpha-phenylglycine methyl ester + 7-aminocephalosporanic acid
methanol + ?
-
-
-
?
D-alpha-phenylglycine methyl ester + H2O
D-alpha-phenylglycine + methanol
-
-
-
?
D-alpha-phenylglycine methyl ester + H2O
D-alpha-phenylglycine + methanol
-
-
-
?
D-alpha-phenylglycine methyl ester + H2O
D-alpha-phenylglycine + methanol
-
-
-
?
D-alpha-phenylglycine methyl ester + H2O
D-alpha-phenylglycine + methanol
-
-
-
?
D-methionine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
D-methionine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
D-methionine methyl ester + H2O
D-methionine + methanol
-
-
-
?
D-methionine methyl ester + H2O
D-methionine + methanol
-
-
-
r
D-methionine methyl ester + H2O
D-methionine + methanol
-
-
-
?
D-phenylglycine amide + H2O
D-phenylglycine + NH3
-
-
-
-
?
D-phenylglycine amide + H2O
D-phenylglycine + NH3
-
-
r
D-phenylglycine amide + H2O
D-phenylglycine + NH3
-
-
-
-
?
D-phenylglycine amide + H2O
D-phenylglycine + NH3
-
-
-
-
?
D-phenylglycine amide + H2O
D-phenylglycine + NH3
-
-
-
-
?
D-phenylglycine amide + H2O
D-phenylglycine + NH3
-
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
r
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
-
?
D-phenylglycine methyl ester + H2O
D-phenylglycine + methanol
-
-
-
-
?
L-cysteine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
L-cysteine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
L-cysteine methyl ester + H2O
L-cysteine + methanol
-
-
-
?
L-cysteine methyl ester + H2O
L-cysteine + methanol
-
-
-
?
L-methionine methyl ester + H2O
L-methionine + methanol
-
-
-
r
L-methionine methyl ester + H2O
L-methionine + methanol
-
-
-
?
L-phenylalanine methyl ester + H2O
L-phenylalanine + methanol
-
-
-
r
L-phenylalanine methyl ester + H2O
L-phenylalanine + methanol
-
-
-
?
L-serine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
L-serine methyl ester + 7-amino-3-deacetoxycephalosporanic acid
methanol + ?
-
-
-
?
L-serine methyl ester + H2O
L-serine + methanol
-
-
-
-
?
L-serine methyl ester + H2O
L-serine + methanol
-
-
-
?
valacyclovir + H2O
?
-
-
-
-
?
valacyclovir + H2O
?
-
stereospecific reaction, the L-isomer is hydrolyzed approximately 20fold faster than the D-isomer
-
-
?
valacyclovir + H2O
?
-
stereospecific reaction
-
-
?
additional information
?
-
-
the enzyme synthesizes ampicillin and artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
the enzyme synthesizes ampicillin and artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
the enzyme synthesizes ampicillin and artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
alpha-amino acid ester hydrolase catalyzes the synthesis of beta-lactam antibiotics, e.g. cefadroxil, cefprozil and cefatrizine, containing an alpha-amino group with decreased activity toward antibiotics with a para-hydroxyl group
-
-
?
additional information
?
-
modeling of enzyme complexes with various substrates to determine substrate specificity
-
-
?
additional information
?
-
-
modeling of enzyme complexes with various substrates to determine substrate specificity
-
-
?
additional information
?
-
-
synthesis of artificial cephalosporins by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters, e.g. synthesis of cefprozil, cefatrizine, and cefadroxil from D-4-hydroxyphenylglycine methyl ester or D-oxyphenylglycine methyl ester and 7-amino-3-propenylcephalosporanic acid, 7-amino-3-[(1H-1,2,3-triazol-4-ylthio)methyl]-cephalosporanic acid, or 7-amino-3-desacetoxy cephalosporanic acid, substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
the enzyme possesses high specificity to esters containing an amino group as a substituent on the Calpha atom of the acid, and it is capable to catalyze N-acylation of 7-aminocephem and 6-aminopenam by these esters with the formation of an amide bond. Synthesis of amino-beta-lactam antibiotic cephalexin from the key intermediate 7-aminodesacetoxycephalosporanic acid and the acylating agent of D-phenylglycine methyl ester by the recombinant enzyme in cell-free extract produced in Escherichia coli VKPM B-11246 is more efficient in comparison with the wild-type enzyme in cell-free extract prepared from mutant strain Xanthomonas rubrilineans VKPM B-9915
-
-
?
additional information
?
-
-
the enzyme possesses high specificity to esters containing an amino group as a substituent on the Calpha atom of the acid, and it is capable to catalyze N-acylation of 7-aminocephem and 6-aminopenam by these esters with the formation of an amide bond. Synthesis of amino-beta-lactam antibiotic cephalexin from the key intermediate 7-aminodesacetoxycephalosporanic acid and the acylating agent of D-phenylglycine methyl ester by the recombinant enzyme in cell-free extract produced in Escherichia coli VKPM B-11246 is more efficient in comparison with the wild-type enzyme in cell-free extract prepared from mutant strain Xanthomonas rubrilineans VKPM B-9915
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
all the L-amino acid 1-[4-(hydroxymethyl)phenyl]guanidine esters are effectively activated in HeLa and Caco-2 cell homogenates and are found to be good substrates of hVACVase. Substrate affinities for human peptide transporter 1, overview
-
-
?
additional information
?
-
-
hVACVase is a prodrug-activating enzyme for amino acid prodrugs including the antiviral drugs valacyclovir and valganciclovir. In hVACVase-catalyzed reactions, the leaving group of the substrate corresponds to the drug moiety of the prodrug, the substrate leaving group affects both, binding and specific activity of hVACVase-catalyzed activation, overview. Effect of the leaving group of a series of valine esters, phenylalanine esters, and a valine amide on the efficiency of hVACVase-mediated prodrug activation. Except for phenylalanine methyl and ethyl esters, all of the ester substrates exhibit a relatively high specificity constant. The valine amide Val-[3-(aminomethyl)phenyl]guanidine exhibits significantly higher Km and lower kcat values compared to the corresponding ester Val-[3-(hydroxymethyl)phenyl]guanidine, indicating poor specificity for hVACVase, overview. While the phenylalanine benzyl and ethyl esters are hVACVase substrates, phenylalanine t-butyl ester is not a substrate
-
-
?
additional information
?
-
-
enzyme-mediated hydrolysis of L- and D-isomers of valine esters of a nucleoside-floxuridine
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
Protaminobacter alboflavus
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
Protaminobacter alboflavus IFO 13221
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
Pseudomonas danceae
-
the enzyme synthesizes artificial cephalosporins by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
Pseudomonas melanogenum
-
the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil
-
-
?
additional information
?
-
Pseudomonas melanogenum
-
the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview
-
-
?
additional information
?
-
Pseudomonas melanogenum
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
Pseudomonas melanogenum ATCC 17808
-
the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil
-
-
?
additional information
?
-
Pseudomonas melanogenum ATCC 17808
-
the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview
-
-
?
additional information
?
-
Pseudomonas melanogenum ATCC 17808
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
Pseudomonas melanogenum IFO 12020
-
the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil
-
-
?
additional information
?
-
Pseudomonas melanogenum IFO 12020
-
the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview
-
-
?
additional information
?
-
Pseudomonas melanogenum IFO 12020
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
Pseudomonas melanogenum KY3987
-
the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil
-
-
?
additional information
?
-
Pseudomonas melanogenum KY3987
-
the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview
-
-
?
additional information
?
-
Pseudomonas melanogenum KY3987
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
Pseudomonas melanogenum KY8540
-
the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil
-
-
?
additional information
?
-
Pseudomonas melanogenum KY8540
-
the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview
-
-
?
additional information
?
-
Pseudomonas melanogenum KY8540
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
substrate specificity of the enzyme, which hydrolyzes valacyclovir and some other aciclovir esters with an alpha-amino group in the acyl radical
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters. No activity with benzylpenicillin
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters. No activity with benzylpenicillin
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters. No activity of the recombinant enzyme with benzylpenicillin and cefradoxil
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters. No activity of the recombinant enzyme with benzylpenicillin and cefradoxil
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
additional information
?
-
-
the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters
-
-
?
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0.009
4-carbamimidamidobenzyl L-isoleucinate
-
pH 7.4, 37°C
0.207
4-carbamimidamidobenzyl L-phenylalaninate
-
pH 7.4, 37°C
0.046
4-carbamimidamidobenzyl L-valinate
-
pH 7.4, 37°C
0.011
4-hydroxy-D-phenylglycine methyl ester
-
pH 6.0, 30°C, recombinant enzyme
5.08
7-amino-3-deacetoxycephalosporanic acid
-
-
0.0017 - 0.00196
cefaloglycin
0.001
cefatrizine
-
below, hydrolysis, pH 6.4, 25°C, recombinant enzyme
0.00179
cefradine
Pseudomonas melanogenum
-
pH 6.0, 37°C
0.00035 - 2.99
cephalexin
1.1
D-2-nitro-5-[(phenylglycyl)amino]benzoic acid
30°C, pH 6.2
63 - 292
D-4-hydroxyphenylglycine methyl ester
40.9
D-alanine methyl ester
-
-
8.26
D-alpha-phenylglycine methyl ester
-
-
0.013 - 13
D-phenylglycine amide
0.0026 - 7
D-phenylglycine methyl ester
2.6
ethyl DL-alpha-amino-n-butyrate
-
-
5
glycine ethyl ester
-
-
0.8
L-valine methyl ester
-
-
4.3
methyl D-alpha-aminophenylacetate
-
-
32.2
methyl DL-alpha-aminoisobutyrate
-
-
24
methyl L-alpha-aminophenylacetate
-
-
0.099
phenylalanine benzyl ester
-
pH 7.4, 37°C, recombinant enzyme
6.7
phenylalanine ethyl ester
-
pH 7.4, 37°C, recombinant enzyme
5.14
phenylalanine methyl ester
-
pH 7.4, 37°C, recombinant enzyme
0.207
phenylalanine [3-(hydroxymethyl)phenyl]guanidine
-
pH 7.4, 37°C, recombinant enzyme
0.5
S-benzyl-L-cysteine ethyl ester
-
-
0.00006 - 0.068
valacyclovir
0.0019
valganciclovir
-
pH 7.4, 37°C, recombinant enzyme
0.014
valine 4-nitrobenzyl ester
-
pH 7.4, 37°C, recombinant enzyme
0.06
valine benzyl ester
-
pH 7.4, 37°C, recombinant enzyme
1.81
valine [3-(aminomethyl)phenyl]guanidine
-
pH 7.4, 37°C, recombinant enzyme
0.046
valine [3-(hydroxymethyl)phenyl]guanidine
-
pH 7.4, 37°C, recombinant enzyme
additional information
additional information
-
0.0026
amoxicillin
-
pH 6.0, 30°C, recombinant enzyme
2.6
amoxicillin
30°C, pH 6.2
0.0006
ampicillin
-
pH 6.1, 25°C
0.0006
ampicillin
-
hydrolysis, pH 6.2, 27-30°C
0.001
ampicillin
-
pH 6.0, 30°C, recombinant enzyme
0.0011
ampicillin
-
pH 7.0, 25°C, recombinant enzyme
0.0012
ampicillin
-
hydrolysis, pH 6.4, 25°C, recombinant enzyme
0.00434
ampicillin
Pseudomonas melanogenum
-
pH 6.0, 37°C
1
ampicillin
30°C, pH 6.2
0.00034
cefadroxil
-
pH 6.0, 30°C, recombinant enzyme
1.7
cefadroxil
30°C, pH 6.2
0.0017
cefaloglycin
-
pH 6.0, 30°C, recombinant enzyme
0.00196
cefaloglycin
Pseudomonas melanogenum
-
pH 6.0, 37°C
0.00035
cephalexin
-
pH 6.1, 25°C
0.0015 - 0.0037
cephalexin
-
hydrolysis, pH 6.2, 27-30°C
0.00161
cephalexin
Pseudomonas melanogenum
-
pH 6.0, 37°C
0.0017
cephalexin
-
hydrolysis, pH 6.2, 35°C, native enzyme
0.0018
cephalexin
-
hydrolysis, pH 6.4, 25°C, recombinant enzyme
0.0022
cephalexin
-
pH 7.0, 25°C, recombinant enzyme
0.003
cephalexin
-
hydrolysis, pH 6.4, 30°C, native enzyme
0.0093
cephalexin
-
hydrolysis, pH 6.5, 37°C, native enzyme
0.34
cephalexin
30°C, pH 6.2
0.45
cephalexin
-
30°C, pH 7.0
63
D-4-hydroxyphenylglycine methyl ester
-
mutant V1318S, pH 6.2, 30°C
64
D-4-hydroxyphenylglycine methyl ester
-
mutant R87I, pH 6.2, 30°C
82
D-4-hydroxyphenylglycine methyl ester
-
wild-type enzyme, pH 6.2, 30°C
292
D-4-hydroxyphenylglycine methyl ester
-
mutant V175A, pH 6.2, 30°C
0.013
D-phenylglycine amide
-
above, pH 6.2, 27-30°C
13
D-phenylglycine amide
30°C, pH 6.2
0.0026 - 0.003
D-phenylglycine methyl ester
-
cephalexin synthesis, pH 6.2, 30°C
0.0036
D-phenylglycine methyl ester
-
pH 6.1, 25°C
0.0037
D-phenylglycine methyl ester
-
pH 7.0, 25°C, recombinant enzyme
0.004 - 0.0049
D-phenylglycine methyl ester
-
hydrolysis, pH 6.2, 27-30°C
0.0083
D-phenylglycine methyl ester
-
hydrolysis, pH 6.4, 30°C, native enzyme
0.011
D-phenylglycine methyl ester
-
hydrolysis, pH 6.5, 37°C, native enzyme
0.0145
D-phenylglycine methyl ester
-
cephalexin synthesis, pH 6.4, 30°C, native enzyme
0.021
D-phenylglycine methyl ester
-
cephalexin synthesis, pH 6.2, 35°C, native enzyme
0.09
D-phenylglycine methyl ester
-
hydrolysis, pH 6.4, 25°C, recombinant enzyme
1
D-phenylglycine methyl ester
-
7
D-phenylglycine methyl ester
30°C, pH 6.2
0.00006
valacyclovir
-
pH 7.5, 25°C, recombinant enzyme
0.00019
valacyclovir
-
pH 7.4, 37°C, recombinant enzyme
0.00059
valacyclovir
-
pH 7.4, 37°C, recombinant enzyme
0.068
valacyclovir
-
pH 7.4, 37°C
0.068
valacyclovir
-
pH 7.4, 37°C, recombinant enzyme
additional information
additional information
-
kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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physiological function
-
hVACVase is a prodrug-activating enzyme for amino acid prodrugs including the antiviral drugs valacyclovir and valganciclovir
evolution
-
the enzyme belongs to the class of hydrolases with alpha/beta-type folding
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter pasteurianus belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter turbidans belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Flavobacterium sp. belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Gluconobacter suboxydans belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Mycoplana dimorpha belongs to the first group
evolution
Protaminobacter alboflavus
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Protaminobacter alboflavus belongs to the first group
evolution
Pseudomonas danceae
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas danceae belongs to the first group
evolution
Pseudomonas melanogenum
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas oryzae belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas rubrilineans belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas sp. belongs to the first group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The human enzyme belongs to the second group
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The rat enzyme belongs to the second group
evolution
-
the enzyme belongs to the class of hydrolases with alpha/beta-type folding
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group
-
evolution
Pseudomonas melanogenum KY3987
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Flavobacterium sp. belongs to the first group
-
evolution
Protaminobacter alboflavus IFO 13221
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Protaminobacter alboflavus belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas rubrilineans belongs to the first group
-
evolution
Pseudomonas melanogenum IFO 12020
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter pasteurianus belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter turbidans belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Gluconobacter suboxydans belongs to the first group
-
evolution
Pseudomonas melanogenum ATCC 17808
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas rubrilineans belongs to the first group
-
evolution
Pseudomonas melanogenum KY8540
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas oryzae belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter pasteurianus belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter turbidans belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Mycoplana dimorpha belongs to the first group
-
evolution
-
two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas rubrilineans belongs to the first group
-
additional information
key amino acid residues in the active site are the catalytic triad residues Ser175, His341 and Asp308, residues of the oxyanion hole are Tyr83 and Tyr176, and of the carboxylate cluster are carboxylate groups of Asp209, Glu310 and Asp311. The optimal configuration of residues in the active site occurs with a negative net charge -1 in the carboxylate cluster. Molecular dynamics simulations, docking, and three-dimensional structure homology modeling using the structure of the Xanthomonas campestris enzyme, PDB ID 1MPX, overview
additional information
-
key amino acid residues in the active site are the catalytic triad residues Ser175, His341 and Asp308, residues of the oxyanion hole are Tyr83 and Tyr176, and of the carboxylate cluster are carboxylate groups of Asp209, Glu310 and Asp311. The optimal configuration of residues in the active site occurs with a negative net charge -1 in the carboxylate cluster. Molecular dynamics simulations, docking, and three-dimensional structure homology modeling using the structure of the Xanthomonas campestris enzyme, PDB ID 1MPX, overview
additional information
-
the catalytic triad is formed by residues S174, D307, and H340, and the conserved residue Y82 participates in stabilization of the oxyanion hole
additional information
-
the catalytic triad is formed by residues Ser205, Asp338, and His370, the oxyanion hole by residues Tyrll2 andTyr206, and the carboxylate cluster by residues Asp239, Glu340,and Asp341
additional information
-
the catalytic triad is formed by residues Serl22, Asp227, and His255, catalysis involves residues Asp123 and Met52
additional information
-
the catalytic triad is formed by residues Serl22, Asp227, and His255, the acyl pocket by the Asp123 side chain and Tyr175, the oxyanion hole by the Asp123 backbone NH group. The enzyme active center contains a large open groove for the leaving alcohol group of the substrate, the nucleoside-containing group in the hydrolysis of valacyclovir and its analogues
additional information
-
the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction
additional information
-
the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction, this region affects not only the sub strate specificity of the enzyme but also its activity
additional information
-
the catalytic triad is formed by residues Serl75, Asp308, and His341, the oxyanion hole by residues Tyr83 and Tyr176, and the carboxylate cluster by residues Asp209, Glu310, and Asp311
additional information
-
the enzyme active center contains a large open groove for the leaving alcohol group of the substrate, the nucleoside-containing group in the hydrolysis of valacyclovir and its analogues
additional information
Pseudomonas melanogenum
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
additional information
-
the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction, this region affects not only the sub strate specificity of the enzyme but also its activity
-
additional information
Pseudomonas melanogenum KY3987
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
-
additional information
-
the catalytic triad is formed by residues Serl75, Asp308, and His341, the oxyanion hole by residues Tyr83 and Tyr176, and the carboxylate cluster by residues Asp209, Glu310, and Asp311
-
additional information
Pseudomonas melanogenum IFO 12020
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
-
additional information
-
the catalytic triad is formed by residues Ser205, Asp338, and His370, the oxyanion hole by residues Tyrll2 andTyr206, and the carboxylate cluster by residues Asp239, Glu340,and Asp341
-
additional information
Pseudomonas melanogenum ATCC 17808
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
-
additional information
-
the catalytic triad is formed by residues Serl75, Asp308, and His341, the oxyanion hole by residues Tyr83 and Tyr176, and the carboxylate cluster by residues Asp209, Glu310, and Asp311
-
additional information
Pseudomonas melanogenum KY8540
-
the enzyme from strain IFO 12020 contains two active site His residues per subunit
-
additional information
-
the catalytic triad is formed by residues Ser205, Asp338, and His370, the oxyanion hole by residues Tyrll2 andTyr206, and the carboxylate cluster by residues Asp239, Glu340,and Asp341
-
additional information
-
the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction
-
additional information
-
the catalytic triad is formed by residues Serl75, Asp308, and His341, the oxyanion hole by residues Tyr83 and Tyr176, and the carboxylate cluster by residues Asp209, Glu310, and Asp311
-
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Kato, K.; Kawahara, K.; Takahashi, T.; Kakinuma, A.
Purification of alpha-amino acid ester hydrolase from Xanthomonas citri
Agric. Biol. Chem.
44
1069-1074
1980
Gluconobacter oxydans, Acetobacter pasteurianus, Komagataeibacter xylinus, Mycoplana dimorpha, Protaminobacter alboflavus, Stenotrophomonas maltophilia, Pseudomonas melanogenum, Xanthomonas citri, Xanthomonas oryzae
-
brenda
Kato, K.; Kawahara, K.; Takahashi, T.; Kakinuma, A.
Substrate specificity of alpha-amino acid hydrolase from Xanthomonas citri
Agric. Biol. Chem.
44
1075-1081
1980
Xanthomonas citri
-
brenda
Kato, K.
Kinetics of acyl transfer by alpha-amino acid ester hydrolase from Xanthomonas citri
Agric. Biol. Chem.
44
1083-1088
1980
Xanthomonas citri
-
brenda
Takahashi, T.; Yamazaki, Y.; Kato, K.
Substrate specificity of an alpha-amino acid ester hydrolase produced by Acetobacter turbidans A.T.C.C. 9325
Biochem. J.
137
497-503
1974
Acetobacter pasteurianus
brenda
Kleine, R.; Meisel, P.
Occurrence and some properties of a mercuri-activatable amino acid esterase from rat kidney microsomes
FEBS Lett.
37
120-123
1973
Rattus norvegicus
brenda
MacNaugthan, M.D.; Daugulis, A.J.
Importance of enzyme and solvent physical properties for the biocompatibility relationship of alpha-amino acid ester hydrolase
Enzyme Microb. Technol.
15
114-119
1993
Acetobacter pasteurianus
brenda
Barends, T.R.; Dijkstra, B.W.
Acetobacter turbidans alpha-amino acid ester hydrolase: merohedral twinning in P21 obscured by pseudo-translational NCS
Acta Crystallogr. Sect. D
59
2237-2241
2003
Acetobacter pasteurianus
brenda
Polderman-Tijmes, J.J.; Jekel, P.A.; de Vries, E.J.; van Merode, A.E.; Floris, R.; van der Laan, J.M.; Sonke, T.; Janssen, D.B.
Cloning, sequence analysis, and expression in Escherichia coli of the gene encoding an alpha-amino acid ester hydrolase from Acetobacter turbidans
Appl. Environ. Microbiol.
68
211-218
2002
Acetobacter pasteurianus (Q8VRK8), Acetobacter pasteurianus
brenda
Sugihara, A.; Shimada, Y.; Sugihara, S.; Nagao, T.; Watanabe, Y.; Tominaga, Y.
A novel alpha-amino-acid esterase from Bacillus mycoides capable of forming peptides of DD- and DL-configurations
J. Biochem.
130
119-126
2001
Bacillus mycoides
brenda
Polderman-Tijmes, J.J.; Jekel, P.A.; Jeronimus-Stratingh, C.M.; Bruins, A.P.; Van Der Laan, J.M.; Sonke, T.; Janssen, D.B.
Identification of the catalytic residues of alpha-amino acid ester hydrolase from Acetobacter turbidans by labeling and site-directed mutagenesis
J. Biol. Chem.
277
28474-28482
2002
Acetobacter pasteurianus
brenda
Barends, T.R.; Polderman-Tijmes, J.J.; Jekel, P.A.; Hensgens, C.M.; de Vries, E.J.; Janssen, D.B.; Dijkstra, B.W.
The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases
J. Biol. Chem.
278
23076-23084
2003
Xanthomonas citri
brenda
Fernandez-Lafuente, R.; Hernandez-Justiz, O.; Mateo, C.; Terreni, M.; Alonso, J.; Garcia-Lopez, J.L.; Moreno, M.A.; Guisan, J.M.
Stabilization of a tetrameric enzyme (a-amino acid ester hydrolase from Acetobacter turbidans) enables a very improved performance of ampicillin synthesis
J. Mol. Catal. B
11
633-638
2001
Acetobacter pasteurianus
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brenda
Barends, T.R.; Polderman-Tijmes, J.J.; Jekel, P.A.; Williams, C.; Wybenga, G.; Janssen, D.B.; Dijkstra, B.W.
Acetobacter turbidans alpha -Amino Acid Ester Hydrolase: how a single mutation improves an antibiotic-producing enzyme
J. Biol. Chem.
281
5804-5810
2006
Acetobacter pasteurianus (Q8VRK8), Acetobacter pasteurianus
brenda
Lai, L.; Xu, Z.; Zhou, J.; Lee, K.D.; Amidon, G.L.
Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase
J. Biol. Chem.
283
9318-9327
2008
Homo sapiens
brenda
Sun, J.; Dahan, A.; Amidon, G.
Enhancing the intestinal absorption of molecules containing the polar guanidino functionality: A double-targeted prodrug approach
J. Med. Chem.
53
624-632
2010
Homo sapiens
brenda
Sun, J.; Dahan, A.; Walls, Z.F.; Lai, L.; Lee, K.D.; Amidon, G.L.
Specificity of a prodrug-activating enzyme hVACVase: the leaving group effect
Mol. Pharm.
7
2362-2368
2010
Homo sapiens
brenda
Zarubina, S.A.; Uporov, I.V.; Fedorchuk, E.A.; Fedorchuk, V.V.; Sklyarenko, A.V.; Yarotsky, S.V.; Tishkov, V.I.
3D Structure modeling of alpha-amino acid ester hydrolase from Xanthomonas rubrilineans
Acta Naturae
5(4)
62-70
2013
Acidovorax avenae (Q6YBS3), Acidovorax avenae
brenda
Kurochkina, V.; Sklyarenko, A.; Berezina, O.; Yarotskii, S.
alpha-Amino acid ester hydrolases: properties and applications
Appl. Biochem. Microbiol.
49
672-694
2013
Gluconobacter oxydans, Acetobacter pasteurianus, Flavobacterium sp., Homo sapiens, Mycoplana dimorpha, Protaminobacter alboflavus, Pseudomonas melanogenum, Rattus norvegicus, Xanthomonas campestris, Xanthomonas citri, Xanthomonas oryzae, Acidovorax avenae, Xanthomonas sp., Pseudomonas danceae, Xanthomonas campestris IFO 3835, Pseudomonas melanogenum KY3987, Flavobacterium sp. ATCC 9325, Protaminobacter alboflavus IFO 13221, Acidovorax avenae VKPMB-9915, Pseudomonas melanogenum IFO 12020, Acetobacter pasteurianus ATCC 6033, Gluconobacter oxydans ATCC 621, Pseudomonas melanogenum ATCC 17808, Acidovorax avenae CGMCC No. 2339, Pseudomonas melanogenum KY8540, Xanthomonas oryzae IFO 3995, Acetobacter pasteurianus ATCC 9325, Xanthomonas citri IFO 3835, Mycoplana dimorpha IFO 13213, Acidovorax avenae VKM B-629
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brenda
Ye, L.J.; Wang, L.; Pan, Y.; Cao, Y.
Changing the specificity of alpha-amino acid ester hydrolase toward para-hydroxyl cephalosporins synthesis by site-directed saturation mutagenesis
Biotechnol. Lett.
34
1719-1724
2012
Acidovorax avenae
brenda
Sklyarenko, A.; Berezina, O.; Satarova, D.; Fedorchuk, V.; Fedorchuk, E.; Savin, S.; Yarotsky, S.; Tishkov, V.
Recombinant alpha-amino ester acid hydrolase from Xanthomonas rubrilineans VKPM B-9915 is a highly efficient biocatalyst of cephalexin synthesis
Moscow Univ. Chem. Bull.
69
62-67
2014
Acidovorax avenae, Acidovorax avenae VKPM B-9915
-
brenda
Hossain, M.S.; Tanaka, T.; Takagi, K.; Hayashi, J.; Wakayama, M.
Purification and characterization of Stenotrophomonas maltophilia-derived l-amino acid ester hydrolase for synthesizing dipeptide, isoleucyl-tryptophan
3 Biotech
8
173
2018
Stenotrophomonas maltophilia (A0A2Z6IAJ2)
brenda