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 + = 4 S-adenosyl-L-homocysteine +
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
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Engineering
Engineering on EC 2.1.1.215 - tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase
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D130A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E113A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E6A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F134A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F140A
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
H110A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H219A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H274A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I65A
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I85A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K170A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K283A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L60A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N29A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R179A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R192A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R31A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme