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 converting histamine from amino acid L-histidine. This enzyme belongs in the group II pyridoxal-5-phosphate (PLP)-dependent decarboxylase family [1][2][3]. As the name suggested, this enzyme catalyzes the production of histamine by the removal of carboxylate group from the amino acid L-histidine whilst utilize pyridoxal phosphate as a cofactor [pdf]. The mammalian Histamine decarboxylase is originated from HDC gene which encodes a 74kDa precursor polypeptide[pdf, jbc]. However, the enzyme becomes active when its C-terminal is truncated into 54kDa during post-translation process [pdf, jbc, Taguchi, Ohmori].

Contents


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

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General Information

Histidine Decarboxylase

Symbol: HDC [4e10]

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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