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Literature summary for 2.6.1.1 extracted from

  • Izard, T.; Fol, B.; Paupit, R.A.; Jansonius, J.N.
    Trigonal crystals of porcine mitochondrial aspartate aminotransferase (1990), J. Mol. Biol., 215, 341-344.
    View publication on PubMed
Search for more literature for 2.6.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of enzyme-inhibitor complex, sitting drop vapour diffusion method, 4°C, protein solution: 7 mg/ml, polyethylene glycol 4000 11% w/v, 50 mM potassium phosphate, pH 7.5, reservoir solution: polyethylene glycol 4000 22% w/v, 50 mM potassium phosphate, pH 7.5, X-ray structure analysis Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
N-5'-phosphopyridoxyl L-aspartate cofactor analogue binds covalently to the enzyme Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion mitochondrial isoenzyme Sus scrofa 5739
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
 mitochondrial isozyme
-

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of holoenzyme after purification of apoenzyme with the inhibitor N-5'-phosphopyridoxyl L-aspartate Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
 Sus scrofa oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Sus scrofa oxaloacetate + L-glutamate
-
 r