Histidine decarboxylase

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Histidine decarboxylase
Properties of human protein
Mass / length primary structure 662 amino acids
Secondary to quaternary structure Homodimer
Cofactor Pyridoxal phosphate
Identifier
Gene name HDC
External IDs
Enzyme classification
EC, category 4.1.1.22 lyase
Response type Decarboxylation
Substrate L -histidine
Products histamine
Occurrence
Homology family Decarboxylase
Parent taxon Animals, bacteria
Orthologue
human House mouse
Entrez 3067 15186
Ensemble ENSG00000140287 ENSMUSG00000027360
UniProt P19113 P23738
Refseq (mRNA) NM_001306146 NM_008230
Refseq (protein) NP_001293075 NP_032256
Gene locus Chr 15: 50.24 - 50.27 Mb Chr 2: 126.59 - 126.62 Mb
PubMed search 3067 15186

The histidine decarboxylase (abbreviated HDC ) is an enzyme , the formation of the biogenic amine and neurotransmitter histamine by elimination of carbon dioxide ( decarboxylation ) of histidine catalyzed . Pyridoxal phosphate (active form of pyridoxine ) bound to the enzyme as a prosthetic group is involved in the catalyzed reaction as a cofactor . The enzymatic decarboxylation of histidine with the aid of histidine decarboxylase, which is the first step in the breakdown of the amino acid histidine and the last in histamine biosynthesis, takes place in animals, plants and many bacteria .

Catalyzed reaction

C 6 H 9 N 3 O 2C 5 H 9 N 3 + CO 2

Conversion of histidine to histamine by the enzyme histidine decarboxylase

Individual evidence

  1. UniProt P19113
  2. HM Epps: Studies on bacterial amino-acid decarboxylases: 4. l (-) - histidine decarboxylase from Cl. welchii type A . In: The Biochemical Journal . tape 39 , no. 1 , 1945, ISSN  0264-6021 , p. 42-46 , PMID 16747851 , PMC 1258146 (free full text).
  3. E. Sandmeier, TI Hale, P. Christen: Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases . In: European Journal of Biochemistry . tape 221 , no. 3 , May 1, 1994, ISSN  0014-2956 , pp. 997-1002 , PMID 8181483 .

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