We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
oxaloacetate keto-enol tautomerase, oat-1, oxaloacetate tautomerase, oat-2,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
High-molecular mass oxalacetate tautomerase
-
-
-
-
Oxalacetic keto-enol isomerase
-
-
-
-
Oxaloacetate keto-enol tautomerase
-
-
-
-
Oxaloacetate tautomerase-1
-
-
-
-
Oxaloacetate tautomerase-2
-
-
-
-
Tautomerase, oxalacetate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
keto-Oxaloacetate = enol-oxaloacetate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
intramolecular oxidoreduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
oxaloacetate keto---enol-isomerase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
keto-Oxaloacetate
Enol-oxaloacetate
additional information
?
-
keto-Oxaloacetate
Enol-oxaloacetate
-
-
-
?
keto-Oxaloacetate
Enol-oxaloacetate
-
-
-
?
keto-Oxaloacetate
Enol-oxaloacetate
-
r
-
?
keto-Oxaloacetate
Enol-oxaloacetate
-
r
-
?
keto-Oxaloacetate
Enol-oxaloacetate
-
-
-
?
keto-Oxaloacetate
Enol-oxaloacetate
-
-
-
?
keto-Oxaloacetate
Enol-oxaloacetate
-
-
-
?
keto-Oxaloacetate
Enol-oxaloacetate
-
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+
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
?
-
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DL-isocitrate
-
inhibits enzyme form OAT-2
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
diphosphate
-
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
diphosphate
-
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Fluorocitrate
-
inhibition of OAT-2, tautomerase reaction and aconitase reaction
Maleate
-
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Acid-labile sulfur
-
enzyme form OAT-2 contains 2 atoms of acid-labile sulfur
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.045 - 220
enol-oxaloacetate
0.068
keto-oxaloacetate
-
enzyme form OAT-1
0.045
enol-oxaloacetate
-
enzyme form OAT-1
220
enol-oxaloacetate
-
enzyme form OAT-2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
26.7 - 45.7
enol-oxaloacetate
3.58
keto-oxaloacetate
-
enzyme form OAT-1, 25°C, pH 9.0
26.7
enol-oxaloacetate
-
enzyme form OAT-2, 25°C, pH 9.0
45
enol-oxaloacetate
-
enzyme form OAT-1, 25°C, pH 9.0
45.7
enol-oxaloacetate
-
enzyme form OAT-1, 25°C, pH 9.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8.5 - 10
-
oxaloacetate tautomerase-1
9
-
oxaloacetate tautomerase-2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
enzyme forms OAT-1 and OAT-2
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
brenda
-
about 30% of the tautomerase activity in the matrix are represented by oxaloacetate tautomerase-1 and about 70% by oxaloacetate tautomerase-2
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FUMA_ECO57
548
0
60298
Swiss-Prot
-
FUMA_ECOL6
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
548
0
60299
Swiss-Prot
-
FUMA_ECOLI
Escherichia coli (strain K12)
548
0
60299
Swiss-Prot
-
FUMA_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
580
0
63825
Swiss-Prot
-
A1K6L7_AZOSB
Azoarcus sp. (strain BH72)
73
0
8077
TrEMBL
-
A1K821_AZOSB
Azoarcus sp. (strain BH72)
126
0
14429
TrEMBL
-
D5DYS2_PRIM1
Priestia megaterium (strain ATCC 12872 / QMB1551)
129
0
14654
TrEMBL
-
M5D6P2_STEMA
126
0
14286
TrEMBL
-
D5DA95_PRIM3
Priestia megaterium (strain DSM 319 / IMG 1521)
129
0
14626
TrEMBL
-
A2SL37_METPP
Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1)
71
0
7725
TrEMBL
-
O29588_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
63
0
6949
TrEMBL
-
A9W9U6_CHLAA
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
72
0
7732
TrEMBL
Mitochondrion (Reliability: 2 )
A9W9V0_CHLAA
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
73
0
8096
TrEMBL
-
Q53WI4_THET8
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
64
0
7415
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
37000
-
enzyme form OAT-1, gel filtration
37000
-
enzyme form OAT-1
80000
-
enzyme form OAT-2, gel filtration
80000
-
enzyme form OAT-2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
monomer
-
1 * 37000, enzyme form OAT-1
monomer
-
1 * 37000, enzyme form OAT-1, SDS-PAGE
monomer
-
1 * 80000, enzyme form OAT-2
monomer
-
1 * 80000, enzyme form OAT-2, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
35
-
40% loss of activity after 10 min
40
-
enzyme form OAT-1: no inactivation
40
-
enzyme form OAT-2: t1/2: about 15 min
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
oxaloacetate tautomerase-1 resists freezing and thawing when dissolved in potassium phosphate buffer, pH 7.8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0°C, oxaloacetate tautomerase-1 is quite stable for several days
-
0°C, oxaloacetate tautomerase-2 gradually loses activity within several days
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
enzyme form OAT-1 and enzyme form OAT-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Annett, R.G.; Kosicki, G.W.
Oxalacetate keto-enol tautomerase. Purification and characterization
J. Biol. Chem.
244
2059-2067
1969
Sus scrofa
brenda
Wesenberg, J.C.; Chaudhari, A.; Annet, R.G.
Localization of oxalacetate keto-enol tautomerase
Can. J. Biochem.
54
233-237
1976
Rattus norvegicus, Sus scrofa
brenda
Johnson, J.D.; Creighton, D.J.; Lambert, M.R.
Stereochemistry and function of oxaloacetate keto-enol tautomerase
J. Biol. Chem.
261
4535-4541
1986
Sus scrofa
brenda
Vinogradov, A.D.; Kotlyar, A.B.; Burov, V.I.; Belikova, Y.O.
Regulation of succinate dehydrogenase and tautomerization of oxaloacetate
Adv. Enzyme Regul.
28
271-280
1989
Bos taurus
brenda
Belikova, Y.O.; Kotlyar, A.B.; Vinogradov, A.D.
Identification of the high-molecular-mass mitochondrial oxaloacetate keto-enol tautomerase as inactive aconitase
FEBS Lett.
246
17-20
1989
Bos taurus
brenda
Belikova, Y.O.; Burov, V.I.; Vinogradov, A.D.
Isolation and properties of oxaloacetate keto-enol tautomerases from bovine heart mitochondria
Biochim. Biophys. Acta
936
10-19
1988
Bos taurus
brenda
Belikova, Y.O.; Kotlyar, A.B.; Vinogradov, A.D.
Oxidation of malate by mitochondrial succinate-ubiquinone reductase
Biochim. Biophys. Acta
936
1-9
1988
Bos taurus
brenda
Select items on the left to see more content.
html completed