This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Amines and Polyamines Biosynthesis|
Some taxa known to possess this pathway include
histamine is a biologically active diamine with important roles in animals. In mammals it is involved in the immune response, gastric secretion, neurotransmission and cell growth. histamine metabolism includes its biosynthesis, degradation, storage, secretion and receptor interaction. Most current anti-histamine drugs interfere with cellular receptor interaction (reviewed in [MoyaGarcia05, Huang08a]). The transport and compartmentalization of histamine in relevant cell types is an important area about which little is currently known [Ogasawara06]. In some mammalian cells, it has been suggested that histamine and polyamine metabolism may be interrelated (reviewed in [Medina05]). See pathway histamine degradation.
The enzyme histidine decarboxylase is responsible for histamine biosynthesis from L-histidine. In humans, L-histidine is considered to be an essential amino acid that must be obtained in the diet, because the human genome lacks L-histidine biosynthetic enzymes [Furst04, Reeds00]. Histidine decarboxylase is of interest as a drug target [MoyaGarcia06] due to the role of histamine in pathological states such as inflammatory, neurological and neuroendocrine diseases, as well as osteoporosis and some neoplasias. However, the mammalian enzyme has not yet been fully structurally characterized due to its instability in purified preparations (reviewed in [MoyaGarcia05]). Histidine decarboxylase knockout mice have been constructed and studied, giving new insights into the role of histamine in physiological processes [Ohtsu03, Fitzpatrick03a, Koncz07]. In Drosophila
In both Gram-negative and Gram-positive bacteria, strains of some species have been shown to produce inducible histidine decarboxylases. These enzymes are responsible for instances of histamine poisoning resulting from the toxic effects of ingesting spoiled food containing high levels of histamine (in [Landete08]). Reports of histamine contamination in food, especially fish [Kanki07] and fermented food including wine [Lucas08], make this a significant economic issue, as well as a significant health risk (in [Bakke05]). As an aid in the assay of histamine in food and wine, a histamine dehydrogenase with high specificity for histamine as substrate has been characterized from Rhizobium sp. [Bakke05].
Physiologically, histidine decarboxylase is thought to have a role in metabolic energy generation and/or pH regulation of growth. In lactobacilli synthesis and secretion of histamine counters the lowering of pH by lactic acid that is produced during growth and allows denser cell growth ([Molenaar93] and in [Schelp01]). In Lactobacillus buchneri the histidine decarboxylase gene cluster was found to contain four genes, one of which (hdcC) encodes a putative histidine/histamine antiporter [Martin05].
About This Pathway
In animals, L-histidine can be taken up by membrane transporters in relevant cell types (reviewed in [Palacin98, Castagna97] and converted to histamine by histidine decarboxylase. During inflammatory reactions, large amounts of histamine are released from effector cells (mast cells and basophils) where it is stored in intracellular granules. Mast cells and basophils contain the highest amounts of histamine and histidine decarboxylase, but other cell types also contain histidine decarboxylase and can release histamine immediately after its synthesis. The enzyme can be modulated by a variety of stimuli in vivo including allograft rejection, infection, inflammation and stimulation by lipopolysaccharide (in [Koncz07] and reviewed in [Schneider02b]).
In mammals and some Gram-negative bacteria (for example Raoultella planticola, Enterobacter aerogenes, Morganella morganii) histidine decarboxylase is a pyridoxal 5'-phosphate-dependent enzyme [Wauters04]. However, some Gram-positive bacteria (for example Lactobacillus sp. 30A, Clostridium perfringens, Tetragenococcus muriaticus, Pediococcus parvulus, Staphylococcus capitis, Oenococcus oeni, Photobacterium damselae) have a histidine decarboxylase that is a pyruvoyl-containing enzyme with a different reaction mechanism [Gallagher89, Konagaya02, delasRivas08, Lucas08, Kanki07]. The mammalian enzymes appear to undergo post-translational proteolysis to produce active forms. Reviewed in [MoyaGarcia05].
Relationship Links: KEGG:PART-OF:map00340
Bakke05: Bakke M, Sato T, Ichikawa K, Nishimura I (2005). "Histamine dehydrogenase from Rhizobium sp.: gene cloning, expression in Escherichia coli, characterization and application to histamine determination." J Biotechnol 119(3);260-71. PMID: 15964650
Burg93: Burg MG, Sarthy PV, Koliantz G, Pak WL (1993). "Genetic and molecular identification of a Drosophila histidine decarboxylase gene required in photoreceptor transmitter synthesis." EMBO J 12(3);911-9. PMID: 8096176
Castagna97: Castagna M, Shayakul C, Trotti D, Sacchi VF, Harvey WR, Hediger MA (1997). "Molecular characteristics of mammalian and insect amino acid transporters: implications for amino acid homeostasis." J Exp Biol 200(Pt 2);269-86. PMID: 9050235
delasRivas08: de las Rivas B, Rodriguez H, Carrascosa AV, Munoz R (2008). "Molecular cloning and functional characterization of a histidine decarboxylase from Staphylococcus capitis." J Appl Microbiol 104(1);194-203. PMID: 17887985
Fitzpatrick03a: Fitzpatrick LA, Buzas E, Gagne TJ, Nagy A, Horvath C, Ferencz V, Mester A, Kari B, Ruan M, Falus A, Barsony J (2003). "Targeted deletion of histidine decarboxylase gene in mice increases bone formation and protects against ovariectomy-induced bone loss." Proc Natl Acad Sci U S A 100(10);6027-32. PMID: 12716972
Kamath91: Kamath AV, Vaaler GL, Snell EE (1991). "Pyridoxal phosphate-dependent histidine decarboxylases. Cloning, sequencing, and expression of genes from Klebsiella planticola and Enterobacter aerogenes and properties of the overexpressed enzymes." J Biol Chem 266(15);9432-7. PMID: 2033044
Kanki07: Kanki M, Yoda T, Tsukamoto T, Baba E (2007). "Histidine decarboxylases and their role in accumulation of histamine in tuna and dried saury." Appl Environ Microbiol 73(5);1467-73. PMID: 17220267
Konagaya02: Konagaya Y, Kimura B, Ishida M, Fujii T (2002). "Purification and properties of a histidine decarboxylase from Tetragenococcus muriaticus, a halophilic lactic acid bacterium." J Appl Microbiol 92(6);1136-42. PMID: 12010554
Koncz07: Koncz A, Pasztoi M, Mazan M, Fazakas F, Buzas E, Falus A, Nagy G (2007). "Nitric oxide mediates T cell cytokine production and signal transduction in histidine decarboxylase knockout mice." J Immunol 179(10);6613-9. PMID: 17982051
Lucas08: Lucas PM, Claisse O, Lonvaud-Funel A (2008). "High frequency of histamine-producing bacteria in the enological environment and instability of the histidine decarboxylase production phenotype." Appl Environ Microbiol 74(3);811-7. PMID: 18065614
Martin05: Martin MC, Fernandez M, Linares DM, Alvarez MA (2005). "Sequencing, characterization and transcriptional analysis of the histidine decarboxylase operon of Lactobacillus buchneri." Microbiology 151(Pt 4);1219-28. PMID: 15817789
Medina05: Medina MA, Correa-Fiz F, Rodriguez-Caso C, Sanchez-Jimenez F (2005). "A comprehensive view of polyamine and histamine metabolism to the light of new technologies." J Cell Mol Med 9(4);854-64. PMID: 16364195
Molenaar93: Molenaar D, Bosscher JS, ten Brink B, Driessen AJ, Konings WN (1993). "Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri." J Bacteriol 175(10);2864-70. PMID: 8387991
MoyaGarcia06: Moya-Garcia AA, Pino-Angeles A, Sanchez-Jimenez F (2006). "New structural insights to help in the search for selective inhibitors of mammalian pyridoxal 5'-phosphate-dependent histidine decarboxylase . 4. Synthesis, metabolism and release of histamine." Inflamm Res 55 Suppl 1;S55-6. PMID: 16547811
Ogasawara06: Ogasawara M, Yamauchi K, Satoh Y, Yamaji R, Inui K, Jonker JW, Schinkel AH, Maeyama K (2006). "Recent advances in molecular pharmacology of the histamine systems: organic cation transporters as a histamine transporter and histamine metabolism." J Pharmacol Sci 101(1);24-30. PMID: 16648665
Schelp01: Schelp E, Worley S, Monzingo AF, Ernst S, Robertus JD (2001). "pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a." J Mol Biol 306(4);727-32. PMID: 11243783
Schneider02b: Schneider E, Rolli-Derkinderen M, Arock M, Dy M (2002). "Trends in histamine research: new functions during immune responses and hematopoiesis." Trends Immunol 23(5);255-63. PMID: 12102747
Bruneau92: Bruneau G, Nguyen VC, Gros F, Bernheim A, Thibault J (1992). "Preparation of a rat brain histidine decarboxylase (HDC) cDNA probe by PCR and assignment of the human HDC gene to chromosome 15." Hum Genet 90(3);235-8. PMID: 1487235
Fleming04: Fleming JV, Fajardo I, Langlois MR, Sanchez-Jimenez F, Wang TC (2004). "The C-terminus of rat L-histidine decarboxylase specifically inhibits enzymic activity and disrupts pyridoxal phosphate-dependent interactions with L-histidine substrate analogues." Biochem J 381(Pt 3);769-78. PMID: 15089748
Fleming04a: Fleming JV, Sanchez-Jimenez F, Moya-Garcia AA, Langlois MR, Wang TC (2004). "Mapping of catalytically important residues in the rat L-histidine decarboxylase enzyme using bioinformatic and site-directed mutagenesis approaches." Biochem J 379(Pt 2);253-61. PMID: 14961766
Gallagher93: Gallagher T, Rozwarski DA, Ernst SR, Hackert ML (1993). "Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a." J Mol Biol 230(2);516-28. PMID: 8464063
Grozinger93: Grozinger KG, Kriwacki RW, Leonare SF, Pitner TP (1993). "A novel stereoselective route to (S)-(+)-α-(fluoromethyl)histidine α-halomethylation of (2R,4S)-3-benzoyl-2-(1,1-dimethylethyl)-1-methyl-4-[(N-tritylimidazol-4'-yl)methyl]-1,3-imidazolidin-5-one. Synthesis and 1H NMR spectroscopy." J. Org. Chem. 58, 709-713.
Guirard87: Guirard BM, Snell EE (1987). "Purification and properties of pyridoxal-5'-phosphate-dependent histidine decarboxylases from Klebsiella planticola and Enterobacter aerogenes." J Bacteriol 169(9);3963-8. PMID: 3114230
Hackert81: Hackert ML, Meador WE, Oliver RM, Salmon JB, Recsei PA, Snell EE (1981). "Crystallization and subunit structure of histidine decarboxylase from Lactobacillus 30a." J Biol Chem 256(2);687-90. PMID: 7451468
Huynh86: Huynh QK, Snell EE (1986). "Pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a. Covalent modifications of aspartic acid 191, lysine 155, and the pyruvoyl group." J Biol Chem 261(10);4389-94. PMID: 3082865
Joseph90: Joseph DR, Sullivan PM, Wang YM, Kozak C, Fenstermacher DA, Behrendsen ME, Zahnow CA (1990). "Characterization and expression of the complementary DNA encoding rat histidine decarboxylase." Proc Natl Acad Sci U S A 87(2);733-7. PMID: 2300558
Komori12: Komori H, Nitta Y, Ueno H, Higuchi Y (2012). "Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase." J Biol Chem 287(34);29175-83. PMID: 22767596
Momany95: Momany C, Ernst S, Ghosh R, Chang NL, Hackert ML (1995). "Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution." J Mol Biol 252(5);643-55. PMID: 7563080
Recsei83: Recsei PA, Huynh QK, Snell EE (1983). "Conversion of prohistidine decarboxylase to histidine decarboxylase: peptide chain cleavage by nonhydrolytic serinolysis." Proc Natl Acad Sci U S A 80(4);973-7. PMID: 6405382
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