Sandbox Reserved 773: Difference between revisions
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= Histidine Decarboxylase = | = Histidine Decarboxylase = | ||
<Structure load='4e1o' size=' | <Structure load='4e1o' size='300' frame='true' align='right' caption='Asymmetrical unit of Histidine Decarboxylase bound to 3 substrate analogs Histidine methyl ester (HME)' scene='Insert optional scene name here' /> | ||
'''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. 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. The mammalian Histamine decarboxylase is originated from HDC gene which encodes a 74kDa precursor polypeptide. However, the enzyme becomes active when its C-terminal is truncated into 54kDa during post-translation process. <ref name=tag>PMID: 6425286</ref> <ref name=mast/> <ref name=metabolism>Schwelberger, Hubert G. "Metabolism of Histamine." ''European Histamine Research Society'' Nov. 2013. Web. 29 Nov. 2013. http://www.ehrs.org.uk/schwelberger.pdf</ref> | '''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. 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. The mammalian Histamine decarboxylase is originated from HDC gene which encodes a 74kDa precursor polypeptide. However, the enzyme becomes active when its C-terminal is truncated into 54kDa during post-translation process. <ref name=tag>PMID: 6425286</ref> <ref name=mast/> <ref name=metabolism>Schwelberger, Hubert G. "Metabolism of Histamine." ''European Histamine Research Society'' Nov. 2013. Web. 29 Nov. 2013. http://www.ehrs.org.uk/schwelberger.pdf</ref> | ||
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== General Information == | == General Information == | ||
'''Histidine Decarboxylase''' | '''Histidine Decarboxylase''' | ||
[[Image:Histidine decarboxylase seq.png|thumb|right|Figure 2. Sequence of Histidine Decarboxylase with its corresponding secondary stuctures <ref name=4e10/>]] | |||
'''Symbol''': HDC | '''Symbol''': HDC | ||
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== Sequence and Structure == | == Sequence and Structure == | ||
Histidine Decarboxylase is considered to be a homo-dimer when one observe its [[biological assembly]]. A homo-dimer is a [[quaternary structure]] formed by two identical monomers or protein chains. In human, three human HDC (hHDC) homo-dimers can be joined together to form a trimer [[asymmetric unit]] <ref name=jbc/> <ref name=xray>PMID: 22684068</ref>. Thus, one can use the nomenclature “trimer of dimer” to suggest the complex might dissociate into smaller subunits before dissociating into monomers. The asymmetrical unit can be seen in Figure 1. Specifically, Cystein-180 and Cystein-418 are primary responsible for the oligomerization process of HDC <ref name=xray/>. | Histidine Decarboxylase is considered to be a homo-dimer when one observe its [[biological assembly]]. A homo-dimer is a [[quaternary structure]] formed by two identical monomers or protein chains. In human, three human HDC (hHDC) homo-dimers can be joined together to form a trimer [[asymmetric unit]] <ref name=jbc/> <ref name=xray>PMID: 22684068</ref>. Thus, one can use the nomenclature “trimer of dimer” to suggest the complex might dissociate into smaller subunits before dissociating into monomers. The asymmetrical unit can be seen in Figure 1. Specifically, Cystein-180 and Cystein-418 are primary responsible for the oligomerization process of HDC <ref name=xray/>. | ||
