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Literature summary for 2.6.1.1 extracted from

  • Lowe, P.N.; Rowe, A.F.
    Aspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase (1985), Biochem. J., 232, 689-695.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.1

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate substrate inhibition at high concentration Trichomonas vaginalis
adipate no inhibition Trichomonas vaginalis
L-glutamate competitive Trichomonas vaginalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.062
-
 2-oxoglutarate 30°C Trichomonas vaginalis
0.96
-
 L-aspartate 30°C Trichomonas vaginalis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
 2 * 44000, mitochondria, SDS-PAGE Trichomonas vaginalis
100000
-
 gel filtration Trichomonas vaginalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + 2-oxoglutarate Trichomonas vaginalis
-
 oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate Trichomonas vaginalis Bushby
-
 oxaloacetate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Trichomonas vaginalis
-
 Bushby strain
-
Trichomonas vaginalis Bushby
-
 Bushby strain
-

Purification (Commentary)

Purification (Comment) Organism
200-1000fold, copurification with the aromatic amino acid aminotransferase 2.6.1.57 Trichomonas vaginalis

Reaction

Reaction Comment Organism Reaction ID
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate bi bi ping pong reaction kinetic Trichomonas vaginalis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
172
-
 purified enzyme Trichomonas vaginalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + 2-oxoglutarate
-
 Trichomonas vaginalis pyruvate + L-glutamate
-
 ?
L-alanine + 2-oxoglutarate
-
 Trichomonas vaginalis Bushby pyruvate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Trichomonas vaginalis oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Trichomonas vaginalis oxaloacetate + L-glutamate
-
 r
L-aspartate + 2-oxoglutarate
-
 Trichomonas vaginalis Bushby oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Trichomonas vaginalis Bushby oxaloacetate + L-glutamate
-
 r
L-phenylalanine + 2-oxoglutarate
-
 Trichomonas vaginalis 2-oxo-3-phenylpropionic acid + L-glutamate i.e. phenylpyruvate ?
L-tryptophan + 2-oxoglutarate
-
 Trichomonas vaginalis 3-indole-2-oxopropionic acid + L-glutamate
-
 ?
L-tyrosine + 2-oxoglutarate
-
 Trichomonas vaginalis 3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate i.e. 4-hydroxyphenylpyruvate ?
additional information substrate specificity Trichomonas vaginalis ?
-
 ?
additional information no activity with L-cysteine, L-isoleucine, L-leucine, L-valine, L-glutamine, glycine, L-ornithine, L-lysine, L-arginine Trichomonas vaginalis ?
-
 ?
additional information substrate specificity Trichomonas vaginalis Bushby ?
-
 ?
additional information no activity with L-cysteine, L-isoleucine, L-leucine, L-valine, L-glutamine, glycine, L-ornithine, L-lysine, L-arginine Trichomonas vaginalis Bushby ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 44000, mitochondria, SDS-PAGE Trichomonas vaginalis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.8
-
 L-glutamate 30°C, competitive versus L-aspartate Trichomonas vaginalis
6.8
-
 L-glutamate 30°C, competitive versus 2-oxoglutrate Trichomonas vaginalis
30
-
 2-oxoglutarate 30°C, substrate inhibition Trichomonas vaginalis