Histone-arginine N-methyltransferase
Appearance
Histone-arginine N-methyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.1.125 | ||||||||
CAS no. | 445295-80-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Histone-arginine N-methyltransferase (EC 2.1.1.125, histone protein methylase I, nuclear protein (histone) N-methyltransferase, protein methylase I, S-adenosyl-L-methionine:histone-arginine omega-N-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:histone-arginine Nomega-methyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- S-adenosyl-L-methionine + histone-arginine S-adenosyl-L-homocysteine + histone-Nomega-methyl-arginine
The enzyme forms the Nomega-monomethyl- and Nomega,Nomega'-dimethyl.
References
- ^ Rajpurohit, R., Lee, S.O., Paik, W.K., Kim, S. (1994). "Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine: histone-arginine-N-methyltransferase". J. Biol. Chem. 269 (2): 1075–1082. PMID 8288564.
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: CS1 maint: multiple names: authors list (link) - ^ Rawal, N., Rajpurohit, R., Paik, W.K., Kim, S. (1994). "Purification and characterization of S-adenosylmethionine-protein-arginine-N-methyltransferase from rat liver". Biochem. J. 300 (Pt 2): 483–489. PMC 1138188. PMID 8002954.
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: CS1 maint: multiple names: authors list (link)
External links
- Histone-arginine+N-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)