2.1.1.225: tRNA:m4X modification enzyme
This is an abbreviated version!
For detailed information about tRNA:m4X modification enzyme, go to the full flat file.
Reaction
Synonyms
TRM13, Trm13p, tRNA:Xm4 modification enzyme
ECTree
Advanced search results
Substrates Products
Substrates Products on EC 2.1.1.225 - tRNA:m4X modification enzyme
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REACTION DIAGRAM
S-adenosyl-L-methionine + adenosine4 in tRNAHis
S-adenosyl-L-homocysteine + 2'-O-methyladenosine4 in tRNAHis
S-adenosyl-L-methionine + cytidine4 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine4 in tRNAGly(GCC)
S-adenosyl-L-methionine + cytidine4 in tRNAPro
S-adenosyl-L-homocysteine + 2'-O-methylcytidine4 in tRNAPro
S-adenosyl-L-homocysteine + 2'-O-methyladenosine4 in tRNAHis
-
-
-
?
S-adenosyl-L-methionine + adenosine4 in tRNAHis
S-adenosyl-L-homocysteine + 2'-O-methyladenosine4 in tRNAHis
the enzyme is necessary and sufficient for 2'-O-methylation at position 4 of yeast tRNA. 2'-O-methylation in the acceptor stem of tRNA
-
-
?
S-adenosyl-L-homocysteine + 2'-O-methylcytidine4 in tRNAGly(GCC)
-
-
-
?
S-adenosyl-L-methionine + cytidine4 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine4 in tRNAGly(GCC)
the enzyme is necessary and sufficient for 2'-O-methylation at position 4 of yeast tRNA. 2'-O-methylation in the acceptor stem of tRNA
-
-
?
S-adenosyl-L-homocysteine + 2'-O-methylcytidine4 in tRNAPro
-
-
-
?
S-adenosyl-L-methionine + cytidine4 in tRNAPro
S-adenosyl-L-homocysteine + 2'-O-methylcytidine4 in tRNAPro
the enzyme is necessary and sufficient for 2'-O-methylation at position 4 of yeast tRNA. 2'-O-methylation in the acceptor stem of tRNA
-
-
?
?
-
Trm13p belongs to the RFM superfamily of MTases despite the absence of a significant sequence similarity to previously characterized members of this superfamily. The model reveals residues potentially responsible for cofactor binding, tRNA binding, and catalysis of the 2'-O-methylation reaction. The model suggests a presence of one to three disulfide bonds and/or metal ion binding site next to the substrate binding pocket
-
-
?
additional information
?
-
-
Trm13p belongs to the RFM superfamily of MTases despite the absence of a significant sequence similarity to previously characterized members of this superfamily. The model reveals residues potentially responsible for cofactor binding, tRNA binding, and catalysis of the 2'-O-methylation reaction. The model suggests a presence of one to three disulfide bonds and/or metal ion binding site next to the substrate binding pocket
-
-
?