Information on EC 5.3.2.2 - oxaloacetate tautomerase

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The expected taxonomic range for this enzyme is: Eutheria

EC NUMBER
COMMENTARY hide
5.3.2.2
-
RECOMMENDED NAME
GeneOntology No.
oxaloacetate tautomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
keto-Oxaloacetate = enol-oxaloacetate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
oxaloacetate keto---enol-isomerase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37318-45-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
-
acetoacetate
-
-
citrate
-
-
CuCl2
-
-
Diethyloxaloacetate
-
-
diphosphate
DL-isocitrate
-
inhibits enzyme form OAT-2
DL-malic acid
-
-
Fluorocitrate
HgCl2
-
-
KCl
-
-
Lactate
-
-
LiCl
-
-
Maleate
malonate
MgCl2
-
-
NaCl
-
-
oxalate
Oxaloacetic acid diethylester
-
enzyme form OAT-1 is inhibited, enzyme form OAT-2 not
PCMB
-
-
phenylpyruvate
-
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
phosphoenolpyruvate
-
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
pyruvate
-
-
Urea
-
-
ZnCl2
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Acid-labile sulfur
-
enzyme form OAT-2 contains 2 atoms of acid-labile sulfur
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045 - 220
enol-oxaloacetate
0.068
keto-oxaloacetate
-
enzyme form OAT-1
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26.7 - 45.7
enol-oxaloacetate
3.58
keto-oxaloacetate
Bos taurus
-
enzyme form OAT-1, 25C, pH 9.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.06
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 10
-
oxaloacetate tautomerase-1
9
-
oxaloacetate tautomerase-2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
pH 7.7: about 20% of maximal activity, pH 9.5: about 40% of maximal activity, oxaloacetate tautomerase-2
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
40% loss of activity after 10 min
40
-
enzyme form OAT-1: no inactivation; enzyme form OAT-2: t1/2: about 15 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
oxaloacetate tautomerase-1 resists freezing and thawing when dissolved in potassium phosphate buffer, pH 7.8
-
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme form OAT-1 and enzyme form OAT-2
-
partial
-