In enzymology, a [cytochrome c]-lysine N-methyltransferase (EC 2.1.1.59) is an enzyme that catalyzes the chemical reaction
| [cytochrome c]-lysine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.59 | ||||||||
| CAS no. | 82047-78-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- S-adenosyl-L-methionine + [cytochrome c]-L-lysine S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c-L-lysine, whereas its two products are S-adenosylhomocysteine and cytochrome c-N6-methyl-L-lysine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:[cytochrome c]-L-lysine N6-methyltransferase. Other names in common use include cytochrome c (lysine) methyltransferase, cytochrome c methyltransferase, cytochrome c-specific protein methylase III, cytochrome c-specific protein-lysine methyltransferase, S-adenosyl-L-methionine:[cytochrome c]-L-lysine, and 6-N-methyltransferase. This enzyme participates in lysine degradation.
References
edit- Durban E, Nochumson S, Kim S, Paik WK, Chan SK (1978). "Cytochrome c-specific protein-lysine methyltransferase from Neurospora crassa. Purification, characterization, and substrate requirements". J. Biol. Chem. 253 (5): 1427–35. PMID 203592.
- Nochumson S, Durban E, Kim S, Paik WK (1977). "Cytochrome c-specific protein methylase III from Neurospora crassa". Biochem. J. 165 (1): 11–8. PMC 1164862. PMID 196592.
- Valentine J, Pettigrew GW (1982). "A cytochrome c methyltransferase from Crithidia oncopelti". Biochem. J. 201 (2): 329–38. PMC 1163647. PMID 6282265.
