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Literature summary extracted from

  • Recsei, P.A.; Snell, E.E.
    Histidine decarboxylase from Lactobacillus 30a. Comparative properties of wild type and mutant proenzymes and their derived enzymes (1982), J. Biol. Chem., 257, 7196-7202.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.22 SH-groups wild type and mutant enzyme each contain two SH groups per alpha-chain Lactobacillus sp.

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.22 S51A/G58D mutant enzyme 3 has two amino acid replacements, both in the beta chain: Ser51 is replaced by Ala and Gly58 by Asp. In addition, about 15% of the mutant beta chains contain Met-Ser at the NH2-terminus rather than Ser. These replacements decrease stability of the enzyme and change its pH activity profile, but do not decrease its activity at pH 4.8, its optimum Lactobacillus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.22 1.4
-
 L-His wild-type enzyme Lactobacillus sp.
4.1.1.22 35
-
 L-His mutant enzyme Lactobacillus sp.

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.22 Lactobacillus sp.
-
 wild-type and and mutant enzyme
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.22 L-His
-
 Lactobacillus sp. Histamine + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.22 More a pyruvate-free proenzyme pi-chain, MW: 37000, is converted during activation to a beta-chain, MW 9000, with a carboxy-terminal Ser residue and an alpha-chain, MW: 28000, with a pyruvoyl group blocking the amino-terminus Lactobacillus sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.22 4.8
-
 wild-type and mutant enzyme Lactobacillus sp.