Holocytochrome-c synthase

holocytochrome-c synthase
Holocytochrome-c synthase monomer, Thermus thermophilus
Identifiers
EC no.4.4.1.17
CAS no.75139-03-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Cytochrome c/c1 heme lyase
Identifiers
SymbolCyto_heme_lyase
PfamPF01265
InterProIPR000511
PROSITEPDOC00647
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

holocytochrome c 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.

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