Information on EC 5.3.2.2 - oxaloacetate tautomerase

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The expected taxonomic range for this enzyme is: Eutheria

SplaateEC_Number,Commentary
EC NUMBER
COMMENTARY
5.3.2.2
-
SplaateRecommended_Name,GO_Number
RECOMMENDED NAME
GeneOntology No.
oxaloacetate tautomerase
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SplaateReaction,Reaction_id,Commentary,IF(Commentary != '',Organism,'') ,IF(Commentary != '',Literature,'')
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
keto-Oxaloacetate = enol-oxaloacetate
show the reaction diagram
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-
-
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SplaateReaction_Type,Organism,Commentary,Literature
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
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isomerization
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-
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SplaatePathway,BRENDA_Link,KEGG_Link,MetaCyc_Link,Source_Database
SplaateSystematic_Name,Commentary_IUBMB
SYSTEMATIC NAME
IUBMB Comments
oxaloacetate keto---enol-isomerase
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SplaateSynonyms,Organism,Commentary,Literature
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
High-molecular mass oxalacetate tautomerase
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-
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OAA tautomerase
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-
-
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OAT
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-
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OAT-1
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-
-
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OAT-2
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-
-
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Oxalacetic keto-enol isomerase
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Oxaloacetate keto-enol tautomerase
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-
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Oxaloacetate tautomerase-1
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-
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Oxaloacetate tautomerase-2
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-
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Tautomerase, oxalacetate
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-
-
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SplaateCAS_Registry_Number,Commentary
CAS REGISTRY NUMBER
COMMENTARY
37318-45-9
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SplaateOrganism, Commentary,Literature, Sequence_Code,Sequence_db,Textmining
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme forms OAT-1 and OAT-2
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-
Manually annotated by BRENDA team
SplaateGeneral_Information, Organism, Commentary, Literature
SplaateSubstrates,Products,id,Organism_Substrates,Commentary_Substrates, Literature_Substrates, Commentary_Products, Literature_Products,Reversibility
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
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-
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keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
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-
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keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
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-
-
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keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
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-
-
-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
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-
-
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keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
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r
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-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
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r
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-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
-
proton transfer reaction is not stereospecific
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-
additional information
?
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OAT-2 catalyzes aconitase reaction after treatment with Fe2+ under anaerobic conditions. 3Fe-4S to 4Fe-4S transformation is responsible for aconitase activation. The same catalytic site is involved in the oxaloacetate tautomerase and the aconitase reaction
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-
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additional information
?
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OAT-2 catalyzes aconitase reaction after treatment with Fe2+, significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
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-
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additional information
?
-
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significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
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SplaateNatural_Substrates,Natural_Products,id,Organism_Substrates,Commentary_Substrates,Literature_Substrates,Commentary_Products,Literature_Products,Reversibility
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
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-
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SplaateCofactor,Organism,Commentary,Literature,Filename
SplaateMetals_Ions,Organism,Commentary, Literature
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
-
enzyme form OAT-2 contains 2 atoms of non-heme Fe per mol
Fe
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OAT-2 catalyzes aconitase reaction after treatment with Fe2+ under anaerobic conditions. 3Fe-4S to 4Fe-4S transformation is responsible for aconitase activation
SplaateInhibitors, Organism, Commentary, Literature,Filename
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
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acetoacetate
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citrate
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CuCl2
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Diethyloxaloacetate
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diphosphate
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diphosphate
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enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
DL-isocitrate
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inhibits enzyme form OAT-2
DL-malic acid
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Fluorocitrate
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inhibition of OAT-2, tautomerase reaction and aconitase reaction
Fluorocitrate
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HgCl2
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KCl
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Lactate
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LiCl
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Maleate
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enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Maleate
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malonate
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malonate
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enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
MgCl2
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NaCl
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NEM
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enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
NEM
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enzyme form OAT-2: irreversible loss of oxaloacetate keto-enol tautomerase activity and aconitase activity
oxalate
-
enzyme form OAT-1 is inhibited, enzyme form OAT-2 not
oxalate
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Oxaloacetic acid diethylester
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enzyme form OAT-1 is inhibited, enzyme form OAT-2 not
PCMB
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phenylpyruvate
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enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
phosphoenolpyruvate
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enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
pyruvate
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Urea
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ZnCl2
-
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SplaateActivating_Compound, Organism, Commentary, Literature,Filename
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Acid-labile sulfur
-
enzyme form OAT-2 contains 2 atoms of acid-labile sulfur
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SplaateKM_Value,KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
enol-oxaloacetate
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enzyme form OAT-1
220
enol-oxaloacetate
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enzyme form OAT-2
0.068
keto-oxaloacetate
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enzyme form OAT-1
SplaateTurnover_Number, Turnover_Number_Maximum, Substrate,Organism,Commentary, Literature, Filename
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
26.7
enol-oxaloacetate
Bos taurus
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enzyme form OAT-2, 25C, pH 9.0
45
enol-oxaloacetate
Bos taurus
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enzyme form OAT-1, 25C, pH 9.0
45.7
enol-oxaloacetate
Bos taurus
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enzyme form OAT-1, 25C, pH 9.0
3.58
keto-oxaloacetate
Bos taurus
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enzyme form OAT-1, 25C, pH 9.0
SplaateKCat_KM_Value,KCat_KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
SplaateKI_Value,KI_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
SplaateIC50_Value,IC50_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
SplaateSpecific_Activity, Specific_Activity_Maximum, Organism ,Commentary, Literature
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.06
-
-
SplaatepH_Optimum, pH_Optimum_Maximum, Organism, Commentary, Literature
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 10
-
oxaloacetate tautomerase-1
9
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oxaloacetate tautomerase-2
SplaatepH_Range,pH_Range_Maximum, Organism,Commentary, Literature
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
pH 7.0: about 50% of maximal activity, pH 8.5-10.0: maximal activity, oxaloacetate tautomerase-1
7.7 - 9.5
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pH 7.7: about 20% of maximal activity, pH 9.5: about 40% of maximal activity, oxaloacetate tautomerase-2
SplaateTemperature_Optimum, Temperature_Optimum_Maximum, Organism, Commentary, Literature
SplaateTemperature_Range, Temperature_Range_Maximum, Organism, Commentary, Literature
SplaatepI_Value,pI_Value_Maximum, Organism,Commentary, Literature
SplaateSource_Tissue, Organism, Commentary, Literature, Textmining
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
SplaateLocalization, Organism, Commentary, id_go, Literature, Textmining
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
about 30% of the tautomerase activity in the matrix are represented by oxaloacetate tautomerase-1 and about 70% by oxaloacetate tautomerase-2
Manually annotated by BRENDA team
SplaatePDB,PDB,PDB,Organism,Uniprot_ID
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Methylibium petroleiphilum (strain PM1)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
SplaateMolecular_Weight, Molecular_Weight_Maximum, Organism, Commentary, Literature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
-
enzyme form OAT-1
2877
37000
-
enzyme form OAT-1, gel filtration
2879
55000
-
gel filtration
2876
80000
-
enzyme form OAT-2
2877
80000
-
enzyme form OAT-2, gel filtration
2879
SplaateSubunits, Organism, Commentary, Literature
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 37000, enzyme form OAT-1; 1 * 80000, enzyme form OAT-2
monomer
-
1 * 37000, enzyme form OAT-1, SDS-PAGE; 1 * 80000, enzyme form OAT-2, SDS-PAGE
SplaatePosttranslational_Modification, Organism, Commentary, Literature
SplaateCommentary, Organism, Literature
SplaatepH_Stability,pH_Stability_Maximum, Organism, Commentary, Literature
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
-
quick denaturation below
2874
4
-
at pH 8 or pH 4 more stable than at values in between
2874
8
-
at pH 8 or pH 4 more stable than at values in between
2874
8.5
-
quick denaturation above
2874
SplaateTemperature_Stability,Temperature_Stability_Maximum, Organism, Commentary, Literature
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
-
40% loss of activity after 10 min
2874
40
-
enzyme form OAT-1: no inactivation; enzyme form OAT-2: t1/2: about 15 min
2877
SplaateGeneral_Stability, Organism, Literature
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
oxaloacetate tautomerase-1 resists freezing and thawing when dissolved in potassium phosphate buffer, pH 7.8
-
SplaateOrganic_Solvent, Organism, Commentary, Literature
SplaateOxidation_Stability,Organism,Literature
SplaateStorage_Stability, Organism, Literature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, oxaloacetate tautomerase-1 is quite stable for several days
-
0C, oxaloacetate tautomerase-2 gradually loses activity within several days
-
SplaateCommentary, Organism, Literature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme form OAT-1 and enzyme form OAT-2
-
partial
-
SplaateCommentary, Organism, Literature
SplaateCommentary, Organism, Literature
SplaateEngineering, Organism, Commentary, Literature
SplaateCommentary, Organism, Literature
SplaateApplication,Organism,Commentary,Literature