Any feedback?
Information on EC 5.3.1.13 - arabinose-5-phosphate isomerase
for references in articles please use BRENDA:EC5.3.1.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
5.3.1.13 arabinose-5-phosphate isomeraseIUBMB Comments
The enzyme is involved in the pathway for synthesis of 3-deoxy-D-manno-octulosonate (Kdo), a component of bacterial lipopolysaccharides and plant call walls.
Specify your search results
Word Map
- 5.3.1.13
- kdo
- 3-deoxy-d-manno-octulosonate
- lipopolysaccharide
- lps
- d-ribulose
-
isomerization
- isomerases
- d-ribulose-5-phosphate
-
cmp-kdo
- beta-synthase
-
mime
- cystathionine
-
8-phosphate
-
uropathogenic
-
enediol
-
3-deoxy-d-manno-oct-2-ulosonic
- d-glucitol
-
single-domain
- fragilis
-
k-antigen
The enzyme appears in viruses and cellular organisms
Synonyms
d-arabinose 5-phosphate isomerase, arabinose 5-phosphate isomerase, arabinose-5-phosphate isomerase, a5p isomerase, d-arabinose-5p isomerase, k-api, d-arabinose-5-phosphate isomerase, c3406 protein, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A5P isomerase
API
arabinose 5-phosphate isomerase
Arabinose phosphate isomerase
-
-
-
-
Arabinose phosphate isomerase, arabinose phosphate
-
-
-
-
BF9343_0136
c3406 protein
D-Arabinose 5-phosphate isomerase
D-arabinose-5-phosphate isomerase
D-arabinose-5-phosphate ketol-isomerase
-
-
-
-
G-API
Isomerase, arabinose phosphate
-
-
-
-
K-API
KdsD
KpsF
KPSF protein
L-API
Phosphoarabinoisomerase
-
-
-
-
YrbH
D-Arabinose 5-phosphate isomerase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Arabinose 5-phosphate = D-ribulose 5-phosphate
-
-
-
-
D-Arabinose 5-phosphate = D-ribulose 5-phosphate
mechanism is envisioned to involve an enediol intermediate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
isomerization
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
D-arabinose-5-phosphate aldose-ketose-isomerase
The enzyme is involved in the pathway for synthesis of 3-deoxy-D-manno-octulosonate (Kdo), a component of bacterial lipopolysaccharides and plant call walls.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9023-86-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-deoxy-D-arabinose 5-phosphate
3-deoxy-D-glycero-pentulose 5-phosphate
-
KdsD converts 3-deoxy-A5P to 3-deoxy-Ru5P, but the catalysis proceeds tenfold slower than for the natural substrate isomerization
-
-
?
4-deoxy-D-arabinose 5-phosphate
4-deoxy-D-glycero-pentulose 5-phosphate
-
KdsD converts 4-deoxy-A5P to 4-deoxy-Ru5P, but the catalysis proceeds slower than for the natural substrate isomerization
-
-
?
4-deoxy-D-threo-arabinose 5-phosphate
4-deoxy-D-glycero-pentulose 5-phosphate
the isomerization rate for this compound is 2fold higher than that of the natural substrate
-
-
?
4-deoxy-D-threo-pentofuranose 5-phosphate
4-deoxy-D-glycero-pentulose 5-phosphate
-
the catalytic efficiency is comparable with the natural substrate D-arabinose 5-phosphate
-
-
?
3-deoxy-D-threo-pentofuranose 5-phosphate
3-deoxy-D-glycero-pentulose 5-phosphate
the catalysis proceeds 10fold slower than for the natural substrate isomerization
-
-
?
3-deoxy-D-threo-pentofuranose 5-phosphate
3-deoxy-D-glycero-pentulose 5-phosphate
-
the catalytic efficiency is about 1000times lower than for the natural substrate D-arabinose 5-phosphate
-
-
?
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
-
-
-
?
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
r
-
?
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
r
-
-
?
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
-
-
-
?
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
no activity with D-ribose-5-phosphate, D-arabinose, D-glucose-6-phosphate, D-mannose-6-phosphate, alpha-D-glucose-1-phosphate and D-glucosamine-6-phosphate, Ru5P, no activity with D-ribose-5-phosphate, D-arabinose, D-glucose-6-phosphate, D-mannose-6-phosphate, alpha-D-glucose-1-phosphate and D-glucosamine-6-phosphate
-
r
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
-
Ru5P, no activity with D-ribose-5-phosphate, D-arabinose, D-glucose-6-phosphate, D-mannose-6-phosphate, alpha-D-glucose-1-phosphate and D-glucosamine-6-phosphate
-
r
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
the gut operon is inducible. GutQ is not directly involved in D-glucitol catabolism. The conditional mutant TCM15(DELTAgutQDELTAkdsD) is dependent on exogenous D-arabinose 5-phosphate both for lipopolysaccharide synthesis/growth and for upregulation of the gut operon
-
-
?
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
A5P
Ru5P, no activity with D-ribose-5-phosphate, D-arabinose, D-glucose-6-phosphate, D-mannose-6-phosphate, alpha-D-glucose-1-phosphate and D-glucosamine-6-phosphate
-
r
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
no activity with D-ribose-5-phosphate, D-arabinose, D-glucose-6-phosphate, D-mannose-6-phosphate, alpha-D-glucose-1-phosphate and D-glucosamine-6-phosphate, Ru5P, no activity with D-ribose-5-phosphate, D-arabinose, D-glucose-6-phosphate, D-mannose-6-phosphate, alpha-D-glucose-1-phosphate and D-glucosamine-6-phosphate
-
r
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
A5P
Ru5P, no activity with D-ribose-5-phosphate, D-arabinose, D-glucose-6-phosphate, D-mannose-6-phosphate, alpha-D-glucose-1-phosphate and D-glucosamine-6-phosphate
-
r
D-Ribulose 5-phosphate
?
-
the product arabinose 5-phosphate is the precursor for 2-keto-3-deoxyoctonate, a constituent of a cell wall lipopolysaccharide
-
-
?
D-Ribulose 5-phosphate
?
Escherichia coli B / ATCC 11303
-
the product arabinose 5-phosphate is the precursor for 2-keto-3-deoxyoctonate, a constituent of a cell wall lipopolysaccharide
-
-
?
D-ribulose 5-phosphate
D-arabinose 5-phosphate
-
first enzyme in the biosynthesis of 3-deoxy-D-manno-octulosonate
-
r
D-ribulose 5-phosphate
D-arabinose 5-phosphate
-
-
synthesis of 3-deoxy-D-manno-oct-2-ulosonic acid, biofilm formation
-
r
additional information
?
-
no substrates: D-arabinose, D-arabinose-5-phosphate, D-glucose-6-phosphate, D-mannose-6-phosphate, D-glucosamine-6-phosphate, D-glucose-1-phosphate, and D-ribose-5-phosphate
-
-
?
additional information
?
-
-
no substrates: D-arabinose, D-arabinose-5-phosphate, D-glucose-6-phosphate, D-mannose-6-phosphate, D-glucosamine-6-phosphate, D-glucose-1-phosphate, and D-ribose-5-phosphate
-
-
?
additional information
?
-
-
DL-glyceraldehyde 3-phosphate and D-erythrose 4-phosphate do not serve as alternate substrates
-
?
additional information
?
-
-
key enzyme in synthesis of lipopolysaccharides
-
-
?
additional information
?
-
-
D-ribose 5-phosphate, D-arabinose, D-glucose-6-phosphate, D-mannose 6-phosphate, and D-glucosamine 6-phosphate are no substrates
-
-
?
additional information
?
-
the enzyme does not isomerize D-xylulose-5-phosphate, D-arabinose, D-ribose, and D-ribulose
-
-
?
additional information
?
-
-
D-ribose 5-phosphate, D-arabinose, D-glucose-6-phosphate, D-mannose 6-phosphate, and D-glucosamine 6-phosphate are no substrates
-
-
?
additional information
?
-
-
enzyme is required for 3-deoxy-D-manno-octulosonic acid biosynthesis and for both lipooligosaccharide assembly and capsular polysaccharide expression
-
?
additional information
?
-
-
no activity with D-ribose 5-phosphate
-
-
?
additional information
?
-
KdsD may bind the furanose form of D-arabinose 5-phosphate. The hydroxyl group at C3 and the phosphate group at C5 of the KdsD substrate are important for substrate recognition
-
-
?
additional information
?
-
-
KdsD may bind the furanose form of D-arabinose 5-phosphate. The hydroxyl group at C3 and the phosphate group at C5 of the KdsD substrate are important for substrate recognition
-
-
?
additional information
?
-
KdsD may bind the furanose form of D-arabinose 5-phosphate. The hydroxyl group at C3 and the phosphate group at C5 of the KdsD substrate are important for substrate recognition
-
-
?
additional information
?
-
-
no biofilm formation by the deletion mutant CDY176
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-ribulose 5-phosphate
D-arabinose 5-phosphate
-
first enzyme in the biosynthesis of 3-deoxy-D-manno-octulosonate
-
r
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
the gut operon is inducible. GutQ is not directly involved in D-glucitol catabolism. The conditional mutant TCM15(DELTAgutQDELTAkdsD) is dependent on exogenous D-arabinose 5-phosphate both for lipopolysaccharide synthesis/growth and for upregulation of the gut operon
-
-
?
D-Ribulose 5-phosphate
?
-
the product arabinose 5-phosphate is the precursor for 2-keto-3-deoxyoctonate, a constituent of a cell wall lipopolysaccharide
-
-
?
D-Ribulose 5-phosphate
?
Escherichia coli B / ATCC 11303
-
the product arabinose 5-phosphate is the precursor for 2-keto-3-deoxyoctonate, a constituent of a cell wall lipopolysaccharide
-
-
?
additional information
?
-
-
key enzyme in synthesis of lipopolysaccharides
-
-
?
additional information
?
-
-
enzyme is required for 3-deoxy-D-manno-octulosonic acid biosynthesis and for both lipooligosaccharide assembly and capsular polysaccharide expression
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
Mg2+
Mn2+
Zn2+
additional information
additional information
purified protein does not contain metal ions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytidine 5'-monophospho-3-deoxy-D-manno-2-octulosonic acid
final product of the 3-deoxy-D-manno-2-octulosonic acid biosynthesis pathway
oxido(dioxo)[(2R,3R)-N,2,3-trihydroxy-4-(hydroxy-kO)butanamidato]phosphate(2-)
-
-
Phosphorylated sugars
-
in a series of nonphosphorylated sugars, the order of decreasing inhibitory activity is as follows: aldonic acids, alditols, aldoses
-
[(2R,3R)-1-(hydroxy-kO)-4-(hydroxyamino)-4-oxobutane-2,3-diyl diacetatato](oxido)dioxophosphate(2-)
-
-
[(2R,3R)-2,3-dihydroxy-4-(hydroxy-kO)butanamidato](oxido)dioxophosphate(2-)
-
-
[(4R,5R)-5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl phosphate
-
-
[(4R,5R)-N-hydroxy-5-[(hydroxy-kO)methyl]-2,2-dimethyl-1,3-dioxolane-4-carboxamidato](oxido)dioxophosphate(2-)
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
EDTA treatment increases the activity of c3406 protein by approximately 2.5fold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tetanus
Identification of a d-Arabinose-5-Phosphate Isomerase in the Gram-Positive Clostridium tetani.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
D-arabinose 5-phosphate
-
at 37°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
141
D-arabinose 5-phosphate
-
at 37°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
cytidine 5'-monophospho-3-deoxy-D-manno-2-octulosonic acid
pH 8.5, 37°C
0.035
oxido(dioxo)[(2R,3R)-N,2,3-trihydroxy-4-(hydroxy-kO)butanamidato]phosphate(2-)
-
at 37°C, pH not specified in the publication
0.007
[(2R,3R)-1-(hydroxy-kO)-4-(hydroxyamino)-4-oxobutane-2,3-diyl diacetatato](oxido)dioxophosphate(2-)
-
at 37°C, pH not specified in the publication
0.01
[(2R,3R)-2,3-dihydroxy-4-(hydroxy-kO)butanamidato](oxido)dioxophosphate(2-)
-
at 37°C, pH not specified in the publication
3
[(4R,5R)-N-hydroxy-5-[(hydroxy-kO)methyl]-2,2-dimethyl-1,3-dioxolane-4-carboxamidato](oxido)dioxophosphate(2-)
-
at 37°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
(2R,3R)-2,3-dihydroxy-4-(hydroxyamino)-4-oxobutyl phosphate
Francisella tularensis
-
pH and temperature not specified in the publication
0.01
(2R,3R)-4-amino-2,3-dihydroxy-4-oxobutyl phosphate
Francisella tularensis
-
pH and temperature not specified in the publication
0.007
(2S,3R)-2,3-bis(acetyloxy)-4-(hydroxyamino)-4-oxobutyl phosphate
Francisella tularensis
-
pH and temperature not specified in the publication
3
[(4R,5R)-5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl phosphate
Francisella tularensis
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29.5
-
recombinant wild type enzyme, in Tris·HCl, (pH 8.5, 50 mM), at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7.5
-
only trace A5P isomerase activity observed below pH 5.5 or above pH 7.5
7 - 10
-
pH 7.0: about 70% of maximal activity, pH 10.0: about 70% of maximal activity
7.5 - 8.5
-
about 90% of maximal activity at pH 7.5 and 8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
API is encoded by two paralogous genes kdsD and gutQ, which may substitute for each other
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
a c3406 deletion mutant is still able to compete with wild type CFT073 in a transurethral cochallenge in mice and cannot colonize the mouse kidney
malfunction
-
a c3406 deletion mutant is still able to compete with wild type CFT073 in a transurethral cochallenge in mice and cannot colonize the mouse kidney
-
metabolism
API is a key enzyme in the biosynthesis of lipopolysaccharide, it catalyzes the first reaction of 3-deoxy-d-manno-octulosonate biosynthesis
metabolism
-
the enzyme is involved in the biosynthesis of 3-deoxy-D-manno-oct-2-ulosonic acid and thus of lipopolysaccharide
physiological function
-
the presence of c3406 is not essential for a pathogenic phenotype
physiological function
expression complements the API deficiency of an Escherichia coli API knockout strain
physiological function
expression in Escherichia coli complements an arabinose-5-phosphate isomerase deficient strain
physiological function
-
expression in Escherichia coli complements an arabinose-5-phosphate isomerase deficient strain
-
physiological function
-
the presence of c3406 is not essential for a pathogenic phenotype
-
Show AA Sequence and Transmembrane Helices (10589 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
122000
133000
145000
35000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
trimer or tetramer
?
-
protein exists as polymers, dimers, and monomers in water solution, gel filtration
tetramer
4 * 26000, SDS-PAGE, His-tagged recombinant protein, x * 25740, calculated from sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.7 A resolution, a tetramer of a single-domain sugar isomerase with an endogenous ligand, cytidine 5'-monophosphate-3-deoxy-D-mannooct-2-ulosonate, bound at the active site. Cytidine 5'-monophosphate-3-deoxy-D-mannooct-2-ulosonate corresponds to the end product in the 3-deoxy-D-mannooct-2-ulosonate biosynthetic pathway and presumably acts as a feedback inhibitor
mutant enzyme K59A, sitting drop vapor diffusion method, using 20% PEG 8K and 0.1 M HEPES, pH 7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H88A
the enzyme site-specific mutant is able to catalyze the isomerization of A5P to R5P in vitro with 9.5% of the wild type protein activity
K56A
-
the mutant shows 0.31% residual activity compared to the wild type enzyme
additional information
-
the deletion mutants CDY17615 are transformed with 15 low copy number constructs to study the abilty to biofilms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the recombinant protein by Q-Sepharose fast flow column chromatography
recombinant His-tagged KdsD from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
GutQ. GutQ is a second copy of D-arabinose 5-phosphate isomerase (API) from the genome of Escherichia coli K-12, with biochemical properties similar to those of KdsD
-
kdsD and gutQ, API is encoded by the two paralogous genes, which may substitute for each other, expression of His-tagged KdsD in Escherichia coli strain BL21(DE3), subcloning in strain DH5alpha
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Volk, W.A.
Purification and properties of phosphoarabinoisomerase from Propionibacterium pentosaceum
J. Biol. Chem.
235
1550-1553
1960
Acidipropionibacterium acidipropionici
-
brenda
Volk, W.A.
D-Arabinose 5-phosphate isomerase
Methods Enzymol.
9
585-588
1966
Acidipropionibacterium acidipropionici, Acidipropionibacterium acidipropionici E214
-
brenda
Noltmann, E.A.
Aldose-ketose isomerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
271-354
1972
Escherichia coli, Acidipropionibacterium acidipropionici
-
brenda
Bigham, E.C.; Gragg, Ch.E.; Hall, W.R.; Kelsey, J.E.; Mallory, W.R.; Richardson, C.B.; Benedict, C.; Ray, P.H.
Inhibition of arabinose 5-phosphate isomerase. An approach to the inhibition of bacterial lipopolysaccharide biosynthesis
J. Med. Chem.
27
717-726
1984
Escherichia coli
brenda
Tzeng, Y.L.; Datta, A.; Strole, C.; Kolli, V.S.; Birck, M.R.; Taylor, W.P.; Carlson, R.W.; Woodard, R.W.; Stephens, D.S.
KpsF is the arabinose-5-phosphate isomerase required for 3-deoxy-D-manno-octulosonic acid biosynthesis and for both lipooligosaccharide assembly and capsular polysaccharide expression in Neisseria meningitidis
J. Biol. Chem.
277
24103-24113
2002
Neisseria meningitidis
brenda
Meredith, T.C.; Woodard, R.W.
Escherichia coli YrbH is a D-arabinose 5-phosphate isomerase
J. Biol. Chem.
278
32771-32777
2003
Escherichia coli
brenda
D'Aniello, S.; Spinelli, P.; Ferrandino, G.; Peterson, K.; Tsesarskia, M.; Fisher, G.; D'Aniello, A.
Cephalopod vision involves dicarboxylic amino acids: D-aspartate, L-aspartate and L-glutamate
Biochem. J.
386
331-340
2005
Escherichia coli, Escherichia coli CFT073
brenda
Meredith, T.C.; Woodard, R.W.
Identification of GutQ from Escherichia coli as a D-arabinose 5-phosphate isomerase
J. Bacteriol.
187
6936-6942
2005
Escherichia coli
brenda
Meredith, T.C.; Woodard, R.W.
Characterization of Escherichia coli D-arabinose 5-phosphate isomerase encoded by kpsF: implications for group 2 capsule biosynthesis
Biochem. J.
395
427-432
2006
Escherichia coli (P45395), Escherichia coli, Escherichia coli CFT073 (P45395)
brenda
Tan, L.; Darby, C.
Yersinia pestis YrbH is a multifunctional protein required for both 3-deoxy-D-manno-oct-2-ulosonic acid biosynthesis and biofilm formation
Mol. Microbiol.
61
861-870
2006
Yersinia pestis
brenda
Yeom, S.J.; Kim, N.H.; Park, C.S.; Oh, D.K.
L-ribose production from L-arabinose by using purified L-arabinose isomerase and mannose-6-phosphate isomerase from Geobacillus thermodenitrificans
Appl. Environ. Microbiol.
75
6941-6943
2009
Escherichia coli
brenda
Yep, A.; Sorenson, R.J.; Wilson, M.R.; Showalter, H.D.; Larsen, S.D.; Keller, P.R.; Woodard, R.W.
Enediol mimics as inhibitors of the D-arabinose 5-phosphate isomerase (KdsD) from Francisella tularensis
Bioorg. Med. Chem. Lett.
21
2679-2682
2011
Francisella tularensis
brenda
Airoldi, C.; Sommaruga, S.; Merlo, S.; Sperandeo, P.; Cipolla, L.; Polissi, A.; Nicotra, F.
Targeting bacterial membranes: NMR spectroscopy characterization of substrate recognition and binding requirements of D-arabinose-5-phosphate isomerase
Chemistry
16
1897-1902
2010
Escherichia coli (P45395)
brenda
Mosberg, J.A.; Yep, A.; Meredith, T.C.; Smith, S.; Wang, P.F.; Holler, T.P.; Mobley, H.L.; Woodard, R.W.
A unique arabinose 5-phosphate isomerase found within a genomic island associated with the uropathogenicity of Escherichia coli CFT073
J. Bacteriol.
193
2981-2988
2011
Escherichia coli, Escherichia coli CFT073
brenda
Gourlay, L.J.; Sommaruga, S.; Nardini, M.; Sperandeo, P.; Deho, G.; Polissi, A.; Bolognesi, M.
Probing the active site of the sugar isomerase domain from E. coli arabinose-5-phosphate isomerase via X-ray crystallography
Protein Sci.
19
2430-2439
2010
Escherichia coli (P45395), Escherichia coli
brenda
Airoldi, C.; Sommaruga, S.; Merlo, S.; Sperandeo, P.; Cipolla, L.; Polissi, A.; Nicotra, F.
Targeting bacterial membranes: identification of Pseudomonas aeruginosa D-arabinose-5P isomerase and NMR characterisation of its substrate recognition and binding properties
ChemBioChem
12
719-727
2011
Pseudomonas aeruginosa
brenda
Chiu, H.J.; Grant, J.C.; Farr, C.L.; Jaroszewski, L.; Knuth, M.W.; Miller, M.D.; Elsliger, M.A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Structural analysis of arabinose-5-phosphate isomerase from Bacteroides fragilis and functional implications
Acta Crystallogr. Sect. D
70
2640-2651
2014
Bacteroides fragilis (Q5LIW1), Bacteroides fragilis, Bacteroides fragilis DSM 2151 (Q5LIW1)
brenda
Gabrielli, L.; Merlo, S.; Airoldi, C.; Sperandeo, P.; Gianera, S.; Polissi, A.; Nicotra, F.; Holler, T.P.; Woodard, R.W.; Cipolla, L.
Arabinose 5-phosphate isomerase as a target for antibacterial design studies with substrate analogues and inhibitors
Bioorg. Med. Chem.
22
2576-2583
2014
Pseudomonas aeruginosa (Q9HVW0), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9HVW0)
brenda
Cech, D.; Wang, P.F.; Holler, T.P.; Woodard, R.W.
Analysis of the arabinose-5-phosphate isomerase of Bacteroides fragilis provides insight into regulation of single-domain arabinose phosphate isomerases
J. Bacteriol.
196
2861-2868
2014
Bacteroides fragilis (Q5LIW1), Bacteroides fragilis, Bacteroides fragilis DSM 2151 (Q5LIW1)
brenda
Cech, D.; Markin, K.; Woodard, R.
Identification of a D-arabinose-5-phosphate isomerase in the Gram-positive Clostridium tetani
J. Bacteriol.
199
e00246
2017
Clostridium tetani (A0A4Q0VE60), Clostridium tetani
brenda
Qu, Y.; Zhang, Z.; Wang, C.; Wang, L.; Wu, L.
Expression, purification and characterization of arabinose-5-phosphate isomerase from Arabidopsis thaliana
Sheng Wu Gong Cheng Xue Bao
32
1060-1069
2016
Arabidopsis thaliana
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 5.3.1.13)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
