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Literature summary for 4.1.1.12 extracted from

  • Novogrodsky, A.; Meister, A.
    Control of aspartate beta-decarboxylase activity by transamination (1964), J. Biol. Chem., 239, 879-888.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-oxoglutarate activates Alcaligenes faecalis
2-oxoglutarate Km: 0.0067 mM Alcaligenes faecalis

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Alcaligenes faecalis

Organism

Organism UniProt Comment Textmining
Alcaligenes faecalis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Alcaligenes faecalis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Alcaligenes faecalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Asp highly specific for L-Asp Alcaligenes faecalis L-Ala + CO2
-
?
additional information also catalyzes transamination between 2-oxoglutarate and L-Asp, L-Ala, L-Met, L-Phe, L-Glu, L-Val, L-Leu, L-Ser or L-glutathione Alcaligenes faecalis ?
-
?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate slightly activates. Km in absence of 2-oxoglutarate: 0.2 mM Alcaligenes faecalis