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Literature summary for 2.6.1.11 extracted from

  • Albrecht, A.M.; Vogel, H.J.
    Acetylornithine delta-transaminase. Partial purification and repression behavior (1964), J. Biol. Chem., 239, 1872-1876.
    View publication on PubMed
Search for more literature for 2.6.1.11

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Escherichia coli
additional information not: EDTA Escherichia coli
p-chloromercuribenzoate
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.34
-
 N2-Acetyl-L-ornithine
-
 Escherichia coli
2.5
-
 2-oxoglutarate
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ stimulates Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
-
 Escherichia coli N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
 r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.1
-
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7.1 9.1 pH 7.1: about 70% of activity maximum, pH 9.1: about 15% of activity maximum Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate a pyridoxal phosphate protein Escherichia coli
pyridoxal 5'-phosphate inactive unless pyridoxal 5-phosphate is supplied Escherichia coli
pyridoxal 5'-phosphate Km: 0.0017 mM Escherichia coli