Holocytochrome-c synthase
In enzymology, a holocytochrome-c synthase (EC 4.4.1.17) is an enzyme that catalyzes the chemical reaction
- holocytochrome c
apocytochrome c + heme
Hence, this enzyme has one substrate, holocytochrome c, and two products, apocytochrome c and 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 haem-lyase (CCHL) and cytochrome Cc1 haem-lyase (CC1HL) are mitochondrial enzymes that catalyse the covalent attachment of a haem 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 haem group.[1]
References
- ↑ Zollner A, Rodel G, Haid A (August 1992). "Molecular cloning and characterization of the Saccharomyces cerevisiae CYT2 gene encoding cytochrome-c1-heme lyase". Eur. J. Biochem. 207 (3): 1093–100. doi:10.1111/j.1432-1033.1992.tb17146.x. PMID 1499554.
This article incorporates text from the public domain Pfam and InterPro IPR000511
|
|---|
| | Activity | |
|---|
| | Regulation | |
|---|
| | Classification | |
|---|
| | Types | |
|---|
|