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
5.3.2.2
-
RECOMMENDED NAME
GeneOntology No.
oxaloacetate tautomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
keto-Oxaloacetate = enol-oxaloacetate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
oxaloacetate keto---enol-isomerase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
High-molecular mass oxalacetate tautomerase
-
-
-
-
OAA tautomerase
-
-
-
-
OAT
-
-
-
-
OAT-1
-
-
-
-
OAT-2
-
-
-
-
Oxalacetic keto-enol isomerase
-
-
-
-
Oxaloacetate keto-enol tautomerase
-
-
-
-
Oxaloacetate tautomerase-1
-
-
-
-
Oxaloacetate tautomerase-2
-
-
-
-
Tautomerase, oxalacetate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37318-45-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme forms OAT-1 and OAT-2
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
-
-
-
-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
-
-
-
-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
-
-
-
-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
-
-
-
-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
-
-
-
-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
-
r
-
-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
-
r
-
-
keto-Oxaloacetate
Enol-oxaloacetate
show the reaction diagram
-
proton transfer reaction is not stereospecific
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe
-
enzyme form OAT-2 contains 2 atoms of non-heme Fe per mol
Fe
-
OAT-2 catalyzes aconitase reaction after treatment with Fe2+ under anaerobic conditions. 3Fe-4S to 4Fe-4S transformation is responsible for aconitase activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
-
acetoacetate
-
-
citrate
-
-
Diethyloxaloacetate
-
-
diphosphate
-
-
diphosphate
-
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
DL-isocitrate
-
inhibits enzyme form OAT-2
DL-malic acid
-
-
Fluorocitrate
-
inhibition of OAT-2, tautomerase reaction and aconitase reaction
Fluorocitrate
-
-
Lactate
-
-
Maleate
-
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
-
Maleate
-
-
-
malonate
-
-
malonate
-
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
NEM
-
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
NEM
-
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
-
-
Oxaloacetic acid diethylester
-
enzyme form OAT-1 is inhibited, enzyme form OAT-2 not
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
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Acid-labile sulfur
-
enzyme form OAT-2 contains 2 atoms of acid-labile sulfur
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.045
-
enol-oxaloacetate
-
enzyme form OAT-1
220
-
enol-oxaloacetate
-
enzyme form OAT-2
0.068
-
keto-oxaloacetate
-
enzyme form OAT-1
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
26.7
-
enol-oxaloacetate
-
enzyme form OAT-2, 25C, pH 9.0
45
-
enol-oxaloacetate
-
enzyme form OAT-1, 25C, pH 9.0
45.7
-
enol-oxaloacetate
-
enzyme form OAT-1, 25C, pH 9.0
3.58
-
keto-oxaloacetate
-
enzyme form OAT-1, 25C, pH 9.0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.06
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.5
10
-
oxaloacetate tautomerase-1
9
-
-
oxaloacetate tautomerase-2
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-
pH 7.7: about 20% of maximal activity, pH 9.5: about 40% of maximal activity, oxaloacetate tautomerase-2
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37000
-
-
enzyme form OAT-1
37000
-
-
enzyme form OAT-1, gel filtration
55000
-
-
gel filtration
80000
-
-
enzyme form OAT-2
80000
-
-
enzyme form OAT-2, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
quick denaturation below
4
-
-
at pH 8 or pH 4 more stable than at values in between
8
-
-
at pH 8 or pH 4 more stable than at values in between
8.5
-
-
quick denaturation above
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
oxaloacetate tautomerase-1 resists freezing and thawing when dissolved in potassium phosphate buffer, pH 7.8
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
enzyme form OAT-1 and enzyme form OAT-2
-
partial
-