TRNA (guanine10-N2)-dimethyltransferase

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TRNA (guanine¹⁰-N²)-dimethyltransferase
TRNA (guanine10-N2)-dimethyltransferase
Identifiers
EC no.	2.1.1.213
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

TRNA (guanine¹⁰-N²)-dimethyltransferase (EC 2.1.1.213, PAB1283, N(2),N(2)-dimethylguanosine tRNA methyltransferase, Trm-G10, PabTrm-G10, PabTrm-m2 2G10 enzyme) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine¹⁰-N²)-dimethyltransferase.^[1] This enzyme catalyses the following chemical reaction

2 S-adenosyl-L-methionine + guanine¹⁰ in tRNA

\rightleftharpoons

2 S-adenosyl-L-homocysteine + N²-dimethylguanine¹⁰ in tRNA (overall reaction)

(1a) S-adenosyl-L-methionine + guanine¹⁰ in tRNA

\rightleftharpoons

S-adenosyl-L-homocysteine + N²-methylguanine¹⁰ in tRNA

(1b) S-adenosyl-L-methionine + N²-methylguanine¹⁰ in tRNA

\rightleftharpoons

S-adenosyl-L-homocysteine + N²-dimethylguanine¹⁰ in tRNA

References

^ Armengaud J, Urbonavicius J, Fernandez B, Chaussinand G, Bujnicki JM, Grosjean H (August 2004). "N2-methylation of guanosine at position 10 in tRNA is catalyzed by a THUMP domain-containing, S-adenosylmethionine-dependent methyltransferase, conserved in Archaea and Eukaryota" (PDF). The Journal of Biological Chemistry. 279 (35): 37142–52. doi:10.1074/jbc.m403845200. PMID 15210688.

External links

TRNA+(guanine10-N2)-dimethyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Armengaud J, Urbonavicius J, Fernandez B, Chaussinand G, Bujnicki JM, Grosjean H (August 2004). "N2-methylation of guanosine at position 10 in tRNA is catalyzed by a THUMP domain-containing, S-adenosylmethionine-dependent methyltransferase, conserved in Archaea and Eukaryota" (PDF). The Journal of Biological Chemistry. 279 (35): 37142–52. doi:10.1074/jbc.m403845200. PMID 15210688.

[1]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)