Biology:Holocytochrome-c synthase

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holocytochrome-c synthase
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Holocytochrome-c synthase monomer, Thermus thermophilus
Identifiers
EC number4.4.1.17
CAS number75139-03-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Cytochrome c/c1 heme lyase
Identifiers
SymbolCyto_heme_lyase
PfamPF01265
InterProIPR000511
PROSITEPDOC00647

The enzyme holocytochrome-c synthase (EC 4.4.1.17) catalyzes the chemical reaction

holocytochrome c [math]\displaystyle{ \rightleftharpoons }[/math] apocytochrome c + heme

This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is holocytochrome-c apocytochrome-c-lyase (heme-forming). Other names in common use include cytochrome c heme-lyase, holocytochrome c synthetase, and holocytochrome-c apocytochrome-c-lyase. This enzyme participates in porphyrin and chlorophyll metabolism.

Cytochrome c heme-lyase (CCHL) and cytochrome Cc1 heme-lyase (CC1HL) are mitochondrial enzymes that catalyze the covalent attachment of a heme group on two cysteine residues of cytochrome c and c1. These two enzymes are functionally and evolutionary related. There are two conserved regions, the first is located in the central section and the second in the C-terminal section. Both patterns contain conserved histidine, tryptophan and acidic residues which could be important for the interaction of the enzymes with the apoproteins and/or the heme group.[1]

The human enzyme, HCCS, processes both cytochromes c and c1.[2]

References

  1. "Molecular cloning and characterization of the Saccharomyces cerevisiae CYT2 gene encoding cytochrome-c1-heme lyase". Eur. J. Biochem. 207 (3): 1093–100. August 1992. doi:10.1111/j.1432-1033.1992.tb17146.x. PMID 1499554. 
  2. "Overlapping specificities of the mitochondrial cytochrome c and c1 heme lyases". The Journal of Biological Chemistry 278 (50): 49732–42. December 2003. doi:10.1074/jbc.M308881200. PMID 14514677. 
This article incorporates text from the public domain Pfam and InterPro: IPR000511