BRENDA - Enzyme Database

Arginine decarboxylase from Escherichia coli

Boecker, E.A.; Fischer, E.H.; Snell, E.; J. Biol. Chem. 246, 6776-6781 (1971)

Data extracted from this reference:

Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.1.1.19
Escherichia coli
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.1.19
L-arginine
-
4092
Escherichia coli
agmatine + CO2
-
4092
Escherichia coli
-
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
4.1.1.19
pyridoxal 5'-phosphate
structure of the pyridoxal 5'-phosphate binding site: Ala-Thr-His-Ser-Thr-His-(pyridoxal 5'-phosphate)Lys-Leu-Leu-Asn-Ala-Leu-Ser-Gln-Ala-Ser-Tyr
Escherichia coli
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
4.1.1.19
pyridoxal 5'-phosphate
structure of the pyridoxal 5'-phosphate binding site: Ala-Thr-His-Ser-Thr-His-(pyridoxal 5'-phosphate)Lys-Leu-Leu-Asn-Ala-Leu-Ser-Gln-Ala-Ser-Tyr
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.1.19
L-arginine
-
4092
Escherichia coli
agmatine + CO2
-
4092
Escherichia coli
-