2.1.1.215: tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase
This is an abbreviated version!
For detailed information about tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase, go to the full flat file.
Reaction
4 S-adenosyl-L-methionine
+
Synonyms
EC 2.1.1.32, multisite-specific tRNA methyltransferase, Trm1, Trm1[tRNA (m2(2)G26) methyltransferase], tRNA (m2(2)G26) methyltransferase, tRNA (N2,N2-guanine)-dimethyltransferase, tRNA:m22G26-methyltransferase
ECTree
2.1.1.215 tRNA (guanine26-N2/guanine27-N2)-dimethyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.1.1.215 - tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNACys
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification. A fraction of native tRNACys has a N2-dimethylguanine26/N2-dimethylguanine27 modification. Initially the N2-methylguanine26 modification occurs, and then the second methyl transfer reaction generates N2-dimethylguanine26. The third methyl transfer reaction modifies guanine 27 to N2-methylguanine27 followed by a fourth methylation of N2-methylguanine27 to N2-dimethylguanine27
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe
S-adenosyl-L-methionine + guanine26 in mutant tRNATyr
S-adenosyl-L-homocysteine + N2-methylguanine26 in mutant tRNATyr
mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27
-
-
?
S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26/guanine27 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26/guanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine26/guanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
-
-
?
S-adenosyl-L-methionine + guanine27 in tRNATyr
S-adenosyl-L-homocysteine + N2-methylguanine27 in tRNATyr
wild-type tRNATyr contains the sequence adenine26/guanine27
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-methylguanine27 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/guanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-methylguanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/N2-methylguanine27
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27
-
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/N2-methylguanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in mutant tRNATyr
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in mutant tRNATyr
mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/guanine27 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26/guanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-dimethylguanine26/guanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
-
-
?
S-adenosyl-L-methionine + N2-methylguanine27 in tRNATyr
S-adenosyl-L-homocysteine + N2-dimethylguanine27 in tRNATyr
wild-type tRNATyr contains the sequence adenine26/guanine27
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
the T-arm in tRNA is the binding site of Trm1, multisite specificity, tRNA-docking modeling, overview
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe
-
tRNAPhe from yeast
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe
-
tRNAPhe from yeast
-
-
?
additional information
?
-
-
Aquifex aeolicus TRm1 may recognize only D-stem structure and guanine26 residue
-
-
?
additional information
?
-
recognition mechanisms of the Trm1 proteins: Aquifex aeolicus Trm1 recognizes the guanine26 and guanine27 bases from the T-arm. In contrast, archaeal and eukaryotic Trm1 proteins recognize the guanine26 base from the D-stem and variable region. The distance between the T-arm and guanine26 (or guanine27) is longer than the distance between the D-stem, variable region, and guanine26. These differences from binding site to the target guanine base(s) may decide the multisite or single site recognition of the Trm1 proteins
-
-
?
additional information
?
-
-
recognition mechanisms of the Trm1 proteins: Aquifex aeolicus Trm1 recognizes the guanine26 and guanine27 bases from the T-arm. In contrast, archaeal and eukaryotic Trm1 proteins recognize the guanine26 base from the D-stem and variable region. The distance between the T-arm and guanine26 (or guanine27) is longer than the distance between the D-stem, variable region, and guanine26. These differences from binding site to the target guanine base(s) may decide the multisite or single site recognition of the Trm1 proteins
-
-
?
additional information
?
-
-
yeast tRNAPhe and Escherichia coli tRNALeu transcripts are methylated. In contrast, Escherichia coli tRNASer is not methylated, because this tRNA possesses adenine26 sequence instead of guanine26
-
-
?
additional information
?
-
-
Trm1 catalyzes methyl transfers to class II tRNAs as well as all class I tRNAs, the size and sequence of the variable region are not recognized by Aquifex aeolicus Trm1, all tRNA transcripts are methylated. tRNA recognition mechanism of multisite specific Trm1, Asp132 is a catalytic center, structure-function analysis, overview
-
-
?
