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Literature summary for 4.1.1.22 extracted from

  • Vaaler, G.L.; Recsei, P.A.; Fox, J.L.; Snell, E.E.
    Histidine decarboxylase of Lactobacillus 30a. Comparative sequence of the beta chain from wild type and mutant enzymes (1982), J. Biol. Chem., 257, 12770-12774.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S51A/G58D mutant enzyme Ser51Ala/Gly58Asp shows a significantly increased alpha-helical content and a significant decrease in the isoelectric point of the beta chain, consistent with changes in physical and catalytic properties of the mutant enzyme Lactobacillus sp.

Organism

Organism UniProt Comment Textmining
Lactobacillus sp.
-
-
-
Lactobacillus sp.
-
wilde-type and mutant enzyme
-

Substrates and Products (Substrate)

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