2.1.1.229: tRNA (carboxymethyluridine34-5-O)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (carboxymethyluridine34-5-O)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.229
-
2.1.1.229
-
wobble
-
methyltransferases
-
5-methoxycarbonylmethyluridine
-
ribonucleotide
-
anticodon
-
gene-specific
-
trnagluuuc
-
translationally
-
medicine
- 2.1.1.229
-
wobble
- methyltransferases
-
5-methoxycarbonylmethyluridine
- ribonucleotide
-
anticodon
-
gene-specific
- trnagluuuc
-
translationally
- medicine
Reaction
Synonyms
ABH8, ALKBH8, CmoA, MnmC, Trm9, Trm9-Trm112, Trm9p, TrmC, tRNA methyltransferase 9, YfcK, YML014w
ECTree
Advanced search results
Cofactor
Cofactor on EC 2.1.1.229 - tRNA (carboxymethyluridine34-5-O)-methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
S-adenosyl-S-carboxymethyl-L-homocysteine
i.e. [(3S)-3-amino-3-carboxypropyl]{[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}(carboxymethyl)sulfanium, the enzyme contains a cofactor, S-adenosyl-S-carboxymethyl-L-homocysteine (SCM-SAH), in which the donor methyl group is substituted by a carboxymethyl group. The carboxyl moiety forms a salt-bridge interaction with Arg199 that is conserved in a large group of CmoA-related proteins but is not conserved in other S-adenosyl-L-methionine-containing enzymes. The active site contains one molecule cofactor S-adenosyl-S-carboxymethyl-L-homocysteine per monomer, and not S-adenosyl-L-methionine
-
required for oxidative cleavage of carboxymethyl group from cmnm5U34, FAD-binding site structure, overview
FAD
required for oxidative cleavage of carboxymethyl group from cmnm5U34, FAD-binding site structure, overview
S-adenosyl-L-methionine
-
dependent on, the N-terminal MnmC2 domain is composed of residues 1-245 and contains the SAM binding site. The binding pocket is composed of mostly hydrophobic residues, except for Glu101 and Asp178
S-adenosyl-L-methionine
dependent on, the N-terminal MnmC2 domain is composed of residues 1-245 and contains the SAM binding site. The binding pocket is composed of mostly hydrophobic residues, except for Glu101 and Asp178