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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
-
-
?
3-deoxy-D-threo-pentofuranose 5-phosphate
3-deoxy-D-glycero-pentulose 5-phosphate
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
-
-
?
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
D-ribulose 5-phosphate
D-arabinose 5-phosphate
additional information
?
-
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
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
-
-
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
-
r
-
-
?
D-Arabinose 5-phosphate
D-Ribulose 5-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
-
r
-
-
?
D-Arabinose 5-phosphate
D-Ribulose 5-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-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
-
-
-
r
D-Arabinose 5-phosphate
D-Ribulose 5-phosphate
-
-
-
-
r
D-Ribulose 5-phosphate
?
-
-
-
-
?
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
?
-
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
-
-
-
r
D-ribulose 5-phosphate
D-arabinose 5-phosphate
-
-
-
r
D-ribulose 5-phosphate
D-arabinose 5-phosphate
-
-
-
?
D-ribulose 5-phosphate
D-arabinose 5-phosphate
-
-
-
r
D-ribulose 5-phosphate
D-arabinose 5-phosphate
-
-
-
-
r
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
-
-
-
-
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
?
-
-
KdsD substrate specificity, overview
-
-
?
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
-
-
?
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(2R,3R)-2,3-dihydroxy-4-(hydroxyamino)-4-oxobutyl phosphate
-
-
(2R,3R)-4-amino-2,3-dihydroxy-4-oxobutyl phosphate
-
-
(2S,3R)-2,3-bis(acetyloxy)-4-(hydroxyamino)-4-oxobutyl phosphate
-
-
cytidine 5'-monophospho-3-deoxy-D-manno-2-octulosonic acid
final product of the 3-deoxy-D-manno-2-octulosonic acid biosynthesis pathway
Erythronic acid 4-phosphate
-
best inhibitor
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-)
-
-
Cd2+
-
-
Cd2+
-
0.01 mM, complete inhibition
Cd2+
-
0.01 mM, significant inhibition
Co2+
-
-
Cu2+
-
-
Hg2+
-
0.01 mM, complete inhibition
Hg2+
-
0.01 mM, significant inhibition
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Zn2+
-
-
Zn2+
-
0.01 mM, complete inhibition, IC50: 0.001-0.003 mM
Zn2+
-
0.01 mM, significant inhibition
Zn2+
-
inhibits substrate binding by the enzyme in a reversible manner
Zn2+
Zn2+ inhibits substrate binding in a reversible manner
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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