Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.1.22 extracted from

  • Worley, S.; Schelp, E.; Monzingo, A.F.; Ernst, S.; Robertus, J.D.
    Structure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a (2002), Proteins Struct. Funct. Genet., 46, 321-329.
    View publication on PubMed
Search for more literature for 4.1.1.22

Protein Variants

Protein Variants Comment Organism
D53N/D54N crystal structure of apo-D53N/D54N double mutant and of mutant complexed with the substrate-analog inhibitor histidine methyl ester, crystals are grown at room temperature by hanging-drop vapor diffusion, drops contain 0.005 ml HDC at 12 mg/ml and 0.005 ml of precipitant solution from the well containing 0-15% polyethylene glycol 400, 4-8% polyethylene glycol 4000, 100 mM sodium acetate, pH 4.6, crystals diffract to 3.2 A Lactobacillus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-histidine Lactobacillus sp.
-
 histamine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Lactobacillus sp.
-
 30a
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-histidine
-
 Lactobacillus sp. histamine + CO2
-
 ?

Synonyms

Synonyms Comment Organism
HDC
-
 Lactobacillus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.8
-
 HDC is essentially inactive at neutral and alkaline pH and active at low pH, low pH shifts HDC from the inactive, i.e. T-state, to the active, i.e. R-state Lactobacillus sp.

Cofactor

Cofactor Comment Organism Structure
additional information HDC uses a covalently bound pyruvoyl moiety as cofactor Lactobacillus sp.