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Literature summary extracted from

  • Matsuzawa, T.
    Characteristics of the inhibition of ornithine-delta-aminotransferase by branched-chain amino acids (1974), J. Biochem., 75, 601-609.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.13 L-isoleucine inhibitory action largely depends on the branched structure of the hydrophobic residue Rattus norvegicus
2.6.1.13 L-leucine inhibitory action largely depends on the branched structure of the hydrophobic residue Rattus norvegicus
2.6.1.13 L-valine competitive with L-ornithine; inhibitory action largely depends on the branched structure of the hydrophobic residue Rattus norvegicus
2.6.1.13 norvaline inhibitory action largely depends on the branched structure of the hydrophobic residue Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.13 additional information
-
 additional information
-
 Rattus norvegicus
2.6.1.13 1.4
-
 DL-pyrroline-5-carboxylate
-
 Rattus norvegicus
2.6.1.13 25
-
 L-glutamate
-
 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.13 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.6.1.13 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.13 L-ornithine + 2-oxoglutarate
-
 Rattus norvegicus DELTA1-pyrroline-5-carboxylate + L-glutamate DL-pyrroline-5-carboxylate r

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.13 8
-
-
 Rattus norvegicus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.6.1.13 2
-
 L-valine forward reaction, 37°C, pH 8 Rattus norvegicus
2.6.1.13 20
-
 L-valine reverse reaction, 37°C, pH 8 Rattus norvegicus