Sandbox Reserved 773: Difference between revisions
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'''Vmax''': 1880 nmol/min/mg | '''Vmax''': 1880 nmol/min/mg | ||
[[Image:Histidine decarboxylase seq.png|thumb|right|Figure 2. Sequence of Histidine Decarboxylase with its corresponding secondary stuctures <ref name=4e10/>]] | |||
== 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/>. | ||
