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Literature summary for 2.6.1.13 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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Rattus norvegicus

Ki Value [mM]

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