(cytochrome c)-arginine N-methyltransferase
[cytochrome c]-arginine N-methyltransferase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 2.1.1.124 | ||||||||
CAS no. | 9055-07-6 | ||||||||
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 | ||||||||
|
In enzymology, a [cytochrome c]-arginine N-methyltransferase (EC 2.1.1.124) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + [cytochrome c]-arginine S-adenosyl-L-homocysteine + [cytochrome c]-Nomega-methyl-arginine
Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c-arginine, whereas its two products are S-adenosylhomocysteine and cytochrome c-.
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]-arginine Nomega-methyltransferase. Other names in common use include S-adenosyl-L-methionine:[cytochrome c]-arginine, and omega-N-methyltransferase.
References[]
- Farooqui JZ, Tuck M, Paik WK (1985). "Purification and characterization of enzymes from Euglena gracilis that methylate methionine and arginine residues of cytochrome c". J. Biol. Chem. 260 (1): 537–45. PMID 2981218.
Categories:
- EC 2.1.1
- Enzymes of unknown structure
- EC 2.1 stubs