| holocytochrome-c synthase | |
| Ec Number: | 4.4.1.17 |
| Cas Number: | 75139-03-6 |
| Go Code: | 0004408 |
| Width: | 270 |
| Symbol: | Cyto_heme_lyase |
| Cytochrome c/c1 heme lyase | |
| Pfam: | PF01265 |
| Interpro: | IPR000511 |
| Prosite: | PDOC00647 |
The enzyme holocytochrome-c synthase (EC 4.4.1.17) catalyzes the chemical reaction
holocytochrome c
\rightleftharpoons
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]