Information on EC 5.3.1.12 - Glucuronate isomerase:
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The lowest common taxonomy group for this enzyme is: Bacteria

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EC NUMBERCOMMENTARY
5.3.1.12-

RECOMMENDED NAMEGeneOntology No.
Glucuronate isomeraseGO:0008880

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
D-Glucuronate = D-fructuronate
show the reaction diagram		----
D-Glucuronate = D-fructuronate
show the reaction diagram		reaction mechanisms in which an active site base abstracts the proton from C2 of D-glucuronate to form a cisenediol intermediate. The conjugate acid then transfers this proton to C1 of the cis-enediol intermediate to form D-fructuronateEscherichia coliP0A8G3672186
D-Glucuronate = D-fructuronate
show the reaction diagram		reaction mechanism, overviewBacillus halodurans-702345
D-Glucuronate = D-fructuronate
show the reaction diagram		reaction mechanism, overviewEscherichia coliC6EHQ2702345

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
isomerization----
isomerizationEscherichia coliP0A8G3-672186
isomerizationBacillus halodurans--690912

PATHWAYKEGG LinkMetaCyc Link
beta-D-glucuronide and D-glucuronate degradation-GLUCUROCAT-PWY
D-galacturonate degradation I-GALACTUROCAT-PWY

SYSTEMATIC NAMEIUBMB Comments
D-glucuronate aldose-ketose-isomeraseAlso converts D-galacturonate to D-tagaturonate.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Bh0493Bacillus halodurans--690912, 702345
D-Glucuronate isomerase----
D-glucuronate ketol-isomerase----
Glucuronate isomerase----
Glucuronate isomeraseEscherichia coliP0A8G3-672186
URIBacillus halodurans--702345
URIEscherichia coliC6EHQ2-702345
Uronate isomerase----
Uronate isomeraseEscherichia coli--663305, 702345
Uronate isomeraseEscherichia coliP0A8G3URI672186
Uronate isomeraseBacillus halodurans--690912, 702345
Uronic isomerase----
UxaCEscherichia coliC6EHQ2-702345
Isomerase, glucuronate----
additional informationBacillus halodurans-URI is a member of the amidohydrolase superfamily, AHS702345
additional informationEscherichia coliC6EHQ2URI is a member of the amidohydrolase superfamily, AHS702345

CAS REGISTRY NUMBERCOMMENTARY
9023-87-4-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bacillus halodurans-690912, 702345--Manually annotated by BRENDA team
Escherichia coli-2619, 663305--Manually annotated by BRENDA team
Escherichia coli-672186P0A8G3SWISSPROTManually annotated by BRENDA team
Escherichia coligene uxaC702345C6EHQ2UniProtManually annotated by BRENDA team
Escherichia colistrain K-12, wild type and mutant strains2621--Manually annotated by BRENDA team
Pectobacterium carotovorum-2618--Manually annotated by BRENDA team
Pedobacter heparinus-2620--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
D-Fructuronate?
show the reaction diagram		Escherichia coli-first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism2619---
D-GalacturonateD-Tagaturonate
show the reaction diagram		Escherichia coli--2621---
D-GalacturonateD-Tagaturonate
show the reaction diagram		Pectobacterium carotovorum--2618-2618-
D-GalacturonateD-Tagaturonate
show the reaction diagram		Bacillus halodurans--690912--?
D-GalacturonateD-Tagaturonate
show the reaction diagram		Bacillus halodurans--702345--r
D-GalacturonateD-Tagaturonate
show the reaction diagram		Escherichia coliC6EHQ2-702345--r
D-GalacturonateD-Tagaturonate
show the reaction diagram		Escherichia coli-r2619---
D-GalacturonateD-Tagaturonate
show the reaction diagram		Pedobacter heparinus-r2620---
D-Galacturonate?
show the reaction diagram		Escherichia coli-first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism2619---
D-GlucuronateD-Fructuronate
show the reaction diagram		Escherichia coli--2619, 2621---
D-GlucuronateD-Fructuronate
show the reaction diagram		Escherichia coli--663305--?
D-GlucuronateD-Fructuronate
show the reaction diagram		Pectobacterium carotovorum--2618-2618-
D-GlucuronateD-Fructuronate
show the reaction diagram		Pedobacter heparinus--2620---
D-GlucuronateD-Fructuronate
show the reaction diagram		Bacillus halodurans--690912--?
D-GlucuronateD-Fructuronate
show the reaction diagram		Bacillus halodurans--702345--r
D-GlucuronateD-Fructuronate
show the reaction diagram		Escherichia coliP0A8G3-672186--?
D-GlucuronateD-Fructuronate
show the reaction diagram		Escherichia coliC6EHQ2-702345--r
D-GlucuronateD-Fructuronate
show the reaction diagram		Bacillus halodurans-the mononuclear metal center in the active site is ligated to the C6 carboxylate and the C5 hydroxyl group of the substrate, this hydroxyl group is also hydrogen-bonded to Asp355. The C2 and C3 hydroxyl groups of the substrate are hydrogen bonded to Arg357 and the carbonyl group at C1 is hydrogen bonded to Tyr50702345--r
D-Glucuronate?
show the reaction diagram		Escherichia coli-first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism2619---
D-Tagaturonate?
show the reaction diagram		Escherichia coli-first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism2619---
additional information?-Pedobacter heparinus-the enzyme does not participate in the metabolism of heparin or chondroitin sulfate2620---
additional information?-Bacillus halodurans-active site structure and molecular reaction mechanism, proton transfer from C2 of D-glucuronate to C1 that is initiated by the combined actions of Asp-355 from the end of ?-strand 8 and the C-5 hydroxyl of the substrate that is bound to the metal ion. Formation of the proposed cis-enediol intermediate is further facilitated by the shuttling of the proton between the C2 and C1 oxygens by the conserved Tyr50 and/or Arg355702345---
additional information?-Escherichia coliC6EHQ2chemical mechanism and active site structure, mutational analysis, overview702345---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
D-Fructuronate?
show the reaction diagram		Escherichia coli-first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism2619--
D-GalacturonateD-Tagaturonate
show the reaction diagram		Bacillus halodurans--702345--
D-GalacturonateD-Tagaturonate
show the reaction diagram		Escherichia coliC6EHQ2-702345--
D-Galacturonate?
show the reaction diagram		Escherichia coli-first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism2619--
D-GlucuronateD-Fructuronate
show the reaction diagram		Bacillus halodurans--702345--
D-GlucuronateD-Fructuronate
show the reaction diagram		Escherichia coliC6EHQ2-702345--
D-Glucuronate?
show the reaction diagram		Escherichia coli-first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism2619--
D-Tagaturonate?
show the reaction diagram		Escherichia coli-first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism2619--
additional information?-Pedobacter heparinus-the enzyme does not participate in the metabolism of heparin or chondroitin sulfate2620--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
FADEscherichia coliP0A8G3-672186 2D-image
NADHBacillus halodurans-required702345 2D-image
NADHEscherichia coliC6EHQ2required702345 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Co2+Escherichia coli-stimulation is more potent at lower concentrations than stimulation by Mn2+663305
Mn2+Escherichia coli-maximal stimulation is higher than stimulatipn by Zn2+ or Co2+, stimulation at low concentrations is lower than stimulation by Zn2+ and Co2+663305
Zn2+Escherichia coli-stimulation is more potent at lower concentrations than stimulation by Mn2+. Vmax is about 3times higher in presence of 0.1 mM Mn2+ than in presence of 0.01 mM Zn2+ or Co2+663305
Zn2+Escherichia coliP0A8G3enzyme contains 1 equiv of zinc per subunit672186
Zn2+Bacillus halodurans-contains 0.5 equivalents of Zn2+ per subunit690912
Zn2+Escherichia coliC6EHQ2URI contains up to 1 equivalent702345

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(2S,3R,4S)-4-(hydroxycarbamoyl)-2,3,4-trihydroxybutanoateBacillus halodurans--690912 2D-image
1,10-phenanthrolineEscherichia coli--2619 2D-image
2,2'-dipyridylEscherichia coli--2619 2D-image
2-mercaptoethanolEscherichia coli--2619 2D-image
arabinohydroxamateBacillus halodurans--702345-
Cu2+Escherichia coli--2619 2D-image
cysteineEscherichia coli--2619 2D-image
D-arabinarateBacillus halodurans--702345-
D-arabinaric acidEscherichia coliP0A8G3competitive inhibitor672186 2D-image
D-arabinaric acidBacillus halodurans--690912 2D-image
D-arabinohydroxamateEscherichia coliP0A8G3competitive inhibitor672186 2D-image
EDTAEscherichia coli-0.25 mM, 50% inhibition663305 2D-image
glutathioneEscherichia coli-weak2619 2D-image
L-Gulonic acidEscherichia coliP0A8G3competitive inhibitor672186 2D-image
NaCNEscherichia coli--2619 2D-image
NEMEscherichia coli--2619 2D-image
PCMBEscherichia coli--2619 2D-image
Zn2+Escherichia coli--2619 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.05-D-galacturonateBacillus halodurans-at 30°C, pH 8.0690912 2D-image
0.8-D-galacturonateEscherichia coli-strain Hfr P4X2621 2D-image
1.65-D-galacturonateEscherichia coli--2619 2D-image
0.05-D-glucuronateBacillus halodurans-at 30°C, pH 8.0690912 2D-image
0.05-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H33N702345 2D-image
0.16-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant Y60F702345 2D-image
0.2-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H33A702345 2D-image
0.29-D-glucuronateEscherichia coli-in absence of added metal or chelator663305 2D-image
0.3-D-glucuronateEscherichia coliP0A8G3reconstituted with Co2+, 30°C, pH 8672186 2D-image
0.31-D-glucuronateEscherichia coli-in presence of 0.01 mM Zn2+663305 2D-image
0.4-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant D412A702345 2D-image
0.41-D-glucuronateEscherichia coli-in presence of 0.01 mM Co2+663305 2D-image
0.48-D-glucuronateEscherichia coliP0A8G3reconstituted with Mn2+, 30°C, pH 8672186 2D-image
0.49-D-glucuronateEscherichia coliP0A8G3apoenzyme672186 2D-image
0.5-D-glucuronateEscherichia coliP0A8G3reconstituted with Zn2+, 30°C, pH 8672186 2D-image
0.5-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, wild-type enzyme702345 2D-image
0.55-D-glucuronateEscherichia coliP0A8G3reconstituted with Cd2+, 30°C, pH 8672186 2D-image
0.7-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H59A; pH 8.0, 25°C, mutant H59N702345 2D-image
0.82-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R414K702345 2D-image
0.9-D-glucuronateEscherichia coli-strain Hfr P4X2621 2D-image
1-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant D412N702345 2D-image
1.2-D-glucuronateEscherichia coli-in presence of 0.1 mM Mn2+663305 2D-image
1.3-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant D238N702345 2D-image
1.4-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R414M702345 2D-image
1.7-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant W381F702345 2D-image
2.5-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R302K702345 2D-image
2.6-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R186K702345 2D-image
3.7-D-glucuronateEscherichia coli--2619 2D-image
8.5-D-glucuronateEscherichia coliP0A8G3reconstituted with Ni2+, 30°C, pH 8672186 2D-image
9.4-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H35N702345 2D-image
10.21-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant Y60A702345 2D-image
21-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant W381A702345 2D-image
38-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R186M702345 2D-image
39-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H35A702345 2D-image
56-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H297N702345 2D-image
200-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R302M702345 2D-image
220-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H297A702345 2D-image
0.75-D-TagaturonateEscherichia coli--2619 2D-image
additional information-additional informationEscherichia coliC6EHQ2primary isotope effects on the kinetic constants with D-glucuronate and the effects of changes in solvent viscosity are consistent with product release being the rate-limiting step702345-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2.4-D-galacturonateBacillus halodurans-at 30°C, pH 8.0690912 2D-image
0.6-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant D412N; pH 8.0, 25°C, mutant H33A; pH 8.0, 25°C, mutant H59A702345 2D-image
0.7-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H35A; pH 8.0, 25°C, mutant R414M702345 2D-image
2.1-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H33N702345 2D-image
4-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H35N702345 2D-image
4.7-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R186M702345 2D-image
5.2-D-glucuronateBacillus halodurans-at 30°C, pH 8.0690912 2D-image
5.8-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R414K702345 2D-image
9-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant D412A702345 2D-image
10-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H297A702345 2D-image
13.9-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant Y60A702345 2D-image
15-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H59N702345 2D-image
16-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant W381F702345 2D-image
21.7-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant Y60F702345 2D-image
30-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H297N702345 2D-image
54-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R186K702345 2D-image
60-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant D238N702345 2D-image
160-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R302K702345 2D-image
180-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R302M702345 2D-image
196-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, wild-type enzyme702345 2D-image
250-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant W381A702345 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.018-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H35A7023459213
0.021-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant D412A7023459213
0.043-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H297A7023459213
0.054-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R414M7023459213
0.06-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant D412N7023459213
0.088-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R302M7023459213
0.13-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R186M7023459213
0.43-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H35N7023459213
0.5-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H297N7023459213
0.83-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H59A7023459213
3-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H33A7023459213
7.1-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R414K7023459213
9.5-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant W381F7023459213
12-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant W381A7023459213
21-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H59N; pH 8.0, 25°C, mutant R186K7023459213
46-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant D238N7023459213
47-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant H33N7023459213
63-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant R302K7023459213
66-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant Y60A7023459213
140-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, mutant Y60F7023459213
400-D-glucuronateEscherichia coliC6EHQ2pH 8.0, 25°C, wild-type enzyme7023459213

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0021-(2S,3R,4S)-4-(hydroxycarbamoyl)-2,3,4-trihydroxybutanoateBacillus halodurans-at 30°C, pH 8.0690912 2D-image
1.3e-05-D-arabinaric acidEscherichia coliP0A8G3apo and Zn2+ reconstituted enzyme672186 2D-image
0.0055-D-arabinaric acidBacillus halodurans-at 30°C, pH 8.0690912 2D-image
0.00067-D-arabinohydroxamateEscherichia coliP0A8G3Zn2+ reconstituted enzyme672186 2D-image
0.00093-D-arabinohydroxamateEscherichia coliP0A8G3apo enzyme672186 2D-image
0.00043-L-Gulonic acidEscherichia coliP0A8G3Zn2+ reconstituted enzyme672186 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
additional information-Escherichia coli--2619

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
88.5Escherichia coli--2619
8-Escherichia coliC6EHQ2assay at702345
additional information-Escherichia coliC6EHQ2the pH-rate profiles for kcat and kcat/Km for URI from Escherichia coli are bellshaped and indicate that one group must be unprotonated and another residue must be protonated for catalytic activity702345

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
68.2Pedobacter heparinus-pH 6.0: about 50% of maximal activity at pH 6.0 and 8.22620
69Escherichia coli-pH 6.0: about 30% of maximal activity, pH 9.0: about 40% of maximal activity with D-galacturonate2619
7.59Escherichia coli-pH 7.5: about 55% of maximal activity, pH 9.0: about 75% of maximal activity with glucuronate2619

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Escherichia coliC6EHQ2assay at702345

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
2q01, downloadSCOP (2q01)CATH (2q01)Caulobacter crescentus (strain ATCC 19089 / CB15)
3iac, downloadSCOP (3iac)CATH (3iac)Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
1j5s, downloadSCOP (1j5s)CATH (1j5s)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
49000-Bacillus halodurans-SDS-PAGE690912

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
trimerBacillus halodurans-x-ray crystallography690912
additional informationBacillus halodurans-structure modelling, overview702345
additional informationEscherichia coliC6EHQ2structure modelling using the crystal structure of URI from Bacillus halodurans, overview702345

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
complexed with Zn2+, vapour diffusion method, with 45% polypropylene glycol and 0.1 M Bis-Tris, pH 6.5Bacillus halodurans-690912
enzyme Bh0493 in complex with substrate D-glucuronate, D-fructuronate, or two inhibitory mimics of the cis-enediol intermediate, hanging drop method at room temperature, B16 mg/ml h0493 in 10 mM HEPES, pH 7.5, 150 mM NaCl, 10 mM methionine, 10% glycerol, 1.0 mM DTT, 0.2 mM ZnCl2, and the corresponding substrate or inhibitor at 40 mM, precipitation solutions are 20% PEG 3350 and 0.2 M sodium citrate, pH 6.0, or 25% PEG 3350, 0.1 M Tris, pH 8.5, and 0.2 M NaCl, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolutionBacillus halodurans-702345

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
0-3°C, stable for several months without loss of activityPectobacterium carotovorum-2618
-20°C, stable for at least 6 monthsPedobacter heparinus-2620

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
Resource Q column chromatography and Superdex 200 gel filtrationBacillus halodurans-690912
-Escherichia coli-663305
of the wild type and recombinant protein, ammonium sulfate fractionation, gel filtration, and ion exchange chromatographyEscherichia coliP0A8G3672186
partialEscherichia coli-2619
-Pedobacter heparinus-2620

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expressed in Escherichia coli BL21(DE3) cellsBacillus halodurans-690912
overexpression in Escherichia coliEscherichia coliP0A8G3672186
overexpression in Escherichia coli BL21(DE3)pLysSEscherichia coli-663305

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
D238NEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
D412AEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
D412NEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
H297AEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
H297NEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
H33AEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
H33NEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
H35AEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
H35NEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
H59AEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
R186KEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
R186MEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
R302KEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
R302MEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
R414KEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
R414MEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
W381AEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
W381FEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
Y60AEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
Y60FEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
H59NEscherichia coliC6EHQ2site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme702345
additional informationEscherichia coliC6EHQ2construction of mutants in association with the active site structure of URI from Bacillus halodurans702345

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
2618Kilgore, W.W.; Starr, M.P.Catabolism of galacturonic and glucuronic acids by Erwinia carotovoraJ. Biol. Chem.2342227-22351959Pectobacterium carotovorum PubMed
2619Ashwell, G.; Wahba, A.J.; Hickman, J.Uronic acid metabolism in bacteria: I. Purification and properties of uronic acid isomerase in Echerichia coliJ. Biol. Chem.2351559-15651960Escherichia coli PubMed
2620Karapally, J.C.; Dietrich, C.P.A uronic acid isomerase in Flavobacterium heparinumCan. J. Biochem.48164-1691970Pedobacter heparinus PubMed
2621Portalier, R.C.; Robert-Baudouy, J.M.; Nemoz, G.M.Etudes de mutations affectant les genes de structure de l'isomerase uronique et de l'oxydoreductase altronique chez Escherichia coli K12Mol. Gen. Genet.128301-3191974Escherichia coli PubMed
663305Linster, C.L.; Van Schaftingen, E.A spectrophotometric assay of D-glucuronate based on Escherichia coli uronate isomerase and mannonate dehydrogenaseProtein Expr. Purif.37352-3602004Escherichia coli PubMed
672186Williams, L.; Nguyen, T.; Li, Y.; Porter, T.N.; Raushel, F.M.Uronate isomerase: a nonhydrolytic member of the amidohydrolase superfamily with an ambivalent requirement for a divalent metal ionBiochemistry457453-74622006Escherichia coli PubMed
690912Nguyen, T.T.; Brown, S.; Fedorov, A.A.; Fedorov, E.V.; Babbitt, P.C.; Almo, S.C.; Raushel, F.M.At the periphery of the amidohydrolase superfamily: Bh0493 from Bacillus halodurans catalyzes the isomerization of D-galacturonate to D-tagaturonateBiochemistry471194-12062008Bacillus halodurans PubMed
702345Nguyen, T.T.; Fedorov, A.A.; Williams, L.; Fedorov, E.V.; Li, Y.; Xu, C.; Almo, S.C.; Raushel, F.M.The mechanism of the reaction catalyzed by uronate isomerase illustrates how an isomerase may have evolved from a hydrolase within the amidohydrolase superfamilyBiochemistry488879-88902009Bacillus halodurans, Escherichia coli PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 5.3.1.12)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)