Biology:Histone-arginine N-methyltransferase
From HandWiki
| Histone-arginine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.125 | ||||||||
| CAS number | 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 [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + histone-Nomega-methyl-arginine
The enzyme forms the Nomega-monomethyl- and Nomega,Nomega'-dimethyl.
References
- ↑ "Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase". The Journal of Biological Chemistry 269 (2): 1075–82. January 1994. PMID 8288564.
- ↑ "Purification and characterization of S-adenosylmethionine-protein-arginine N-methyltransferase from rat liver". The Biochemical Journal 300 ( Pt 2) (Pt 2): 483–9. June 1994. doi:10.1042/bj3000483. PMID 8002954.
External links
- Histone-arginine+N-methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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