Sandbox Reserved 773

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This Sandbox is Reserved from Sep 25, 2013, through Mar 31, 2014 for use in the course "BCH455/555 Proteins and Molecular Mechanisms" taught by Michael B. Goshe at the North Carolina State University. This reservation includes Sandbox Reserved 299, Sandbox Reserved 300 and Sandbox Reserved 760 through Sandbox Reserved 779.
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Histidine Decarboxylase

Histidine Decarboxylase (HDC) is an enzyme that is responsible for biosynthesizing histamine from amino acid L-histidine. This enzyme belongs in the group II pyridoxal-5-phosphate (PLP)-dependent decarboxylase family [P19113, PF00282]. As the name suggested, this protein catalyze the production of histamine by the removal of carboxyl group from the amino acid L-histidine whilst utilize pyridoxal phosphate as an active-site cofactor [jbc].

Contents


Model of Histidine Decarboxylase bound to 3 substrate analogs Histidine methyl ester (HME)

Drag the structure with the mouse to rotate

Background

The mammalian Histamine decarboxylase is originated from HDC gene which encodes a 74kDa polypeptide [3067, 1487235]. After post-translation process that truncates C-terminal of the HDC, the enzyme is around 54kDa [4e10, jbc].

General Information

Histidine Decarboxylase

Symbol: HDC

Protein Bank Code: 4E1O

Gene Name: HDC gene

Organism: Homo sapiens

Length: 481 residues

Chains: A, B, C, D, E, F

Molecular Weight: 54314.8

Isoelectric Point: 5.4

Km: 0.1 mM

Vmax: 1880 nmol/min/mg

Structure

Implication

Histidine decarboxylase is responsible for the synthesis of histamine. Histamine is an important key factor for various physiological processes such as gastric acid secretion (3,4), immune response (1,2), cell growth (8-10), and neurotrasmission for appetite, memory, or circadian rhythm (5-7). As a result, any imbalance or distortion of the histamine metabolism can often contribute to a high probability for peptic ulcer, inflammation responses, schizophrenia, or tumor progression (5-7).

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