ID: | 2.1.1.61 |
---|---|
Description: | tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase. |
Cath: | 3.30.9.10; 3.40.50.620; 3.50.50.60; 2.30.30.280; 2.40.30.10; 3.40.50.150; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.1.1.61 |
BRENDA Enzyme Link: | BRENDA 2.1.1.61 |
KEGG Enzyme Link: | KEGG2.1.1.61 |
BioCyc Enzyme Link: | BioCyc 2.1.1.61 |
ExPASy Enzyme Link: | ExPASy2.1.1.61 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.61 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.61 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.61 |
IntEnz Enzyme Link: | IntEnz 2.1.1.61 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.61 |
RHEA:19569 | 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[NH;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Biosynthesis of 5-methylaminomethyl-2-thiouridylate. I. Isolation of a new tRNA-methylase specific for 5-methylaminomethyl-2-thiouridylate. | Taya Y, Nishimura S | 1973 Apr 16 | 4703553 |
Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC. | Kim J, Almo SC | 2013 Apr 24 | 23617613 |
Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA. | Bujnicki JM, Oudjama Y, Roovers M, Owczarek S, Caillet J, Droogmans L | 2004 Aug | 15247431 |