BRENDA - Enzyme Database

Arginine decarboxylase of oats is clipped from a precursor into two polypeptides found in the soluble enzyme

Malmberg, R.L.; Smith, K.E.; Bell, E.; Cellino, M.L.; Plant Physiol. 100, 146-152 (1992)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
4.1.1.19
expression in Escherichia coli
Avena sativa
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.1.1.19
Avena sativa
-
-
-
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
-
4093
Avena sativa
agmatine + CO2
-
4093
Avena sativa
-
Subunits
EC Number
Subunits
Commentary
Organism
4.1.1.19
More
the full-length 66000 MW arginine decarboxylase polypeptide is synthesized and then cleaved to produce a 42000 MW polypeptide containing the original terminus and a 24000 polypeptide containing the original carboxyl terminus. Both of these are found in the enzyme and held together by disulfide bonds
Avena sativa
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
4.1.1.19
expression in Escherichia coli
Avena sativa
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
-
4093
Avena sativa
agmatine + CO2
-
4093
Avena sativa
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.1.1.19
More
the full-length 66000 MW arginine decarboxylase polypeptide is synthesized and then cleaved to produce a 42000 MW polypeptide containing the original terminus and a 24000 polypeptide containing the original carboxyl terminus. Both of these are found in the enzyme and held together by disulfide bonds
Avena sativa