|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Polynucleotide-Reactions → RNA-Reactions → tRNA-Reactions|
EC Number: 22.214.171.124
Enzymes and Genes:
|Escherichia coli K-12 substr. MG1655:||tRNA (Gm18) 2'-O-methyltransferase: trmH|
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: tRNA (guanosine18-2′-O)-methyltransferase
Enzyme Commission Synonyms: tRNA (Gm18) 2'-O-methyltransferase, tRNA (Gm18) methyltransferase, TrmH, SpoU
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -24.902191 [Latendresse13]
Enzyme Commission Summary:
The enzyme catalyses the methylation of guanosine18 in tRNA.
Unification Links: KEGG:R02917
Gefter69: Gefter ML (1969). "The in vitro synthesis of 2'-omethylguanosine and 2-methylthio 6N (gamma,gamma, dimethylallyl) adenosine in transfer RNA of Escherichia coli." Biochem Biophys Res Commun 36(3);435-41. PMID: 4898378
Hori98: Hori H, Yamazaki N, Matsumoto T, Watanabe Y, Ueda T, Nishikawa K, Kumagai I, Watanabe K (1998). "Substrate recognition of tRNA (Guanosine-2'-)-methyltransferase from Thermus thermophilus HB27." J Biol Chem 273(40);25721-7. PMID: 9748240
Kumagai80: Kumagai I, Watanabe K, Oshima T (1980). "Thermally induced biosynthesis of 2'-O-methylguanosine in tRNA from an extreme thermophile, Thermus thermophilus HB27." Proc Natl Acad Sci U S A 77(4);1922-6. PMID: 6990416
Ochi10: Ochi A, Makabe K, Kuwajima K, Hori H (2010). "Flexible recognition of the tRNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes." J Biol Chem 285(12);9018-29. PMID: 20053984
Pleshe05: Pleshe E, Truesdell J, Batey RT (2005). "Structure of a class II TrmH tRNA-modifying enzyme from Aquifex aeolicus." Acta Crystallogr Sect F Struct Biol Cryst Commun 61(Pt 8);722-8. PMID: 16511140
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