2.1.1.34: tRNA (guanosine18-2'-O)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (guanosine18-2'-O)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.34
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2.1.1.34
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thermophilus
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thermus
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d-loops
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ribose
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methyltransferases
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trnaphe
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adomet
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2'-o-methyltransferases
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2'-o-methylguanosine
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analysis
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s-adenosyl-l-homocysteine
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medicine
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methyl-transfer
- 2.1.1.34
- thermophilus
-
thermus
-
d-loops
- ribose
- methyltransferases
- trnaphe
- adomet
-
2'-o-methyltransferases
- 2'-o-methylguanosine
- analysis
- s-adenosyl-l-homocysteine
- medicine
-
methyl-transfer
Reaction
Synonyms
methyltransferase, transfer ribonucleate guanosine 2'-, S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase, SpoU, TARBP1, transfer ribonucleate guanosine 2'-methyltransferase, transfer RNA (Gm18) methyltransferase, TrmH, tRNA (Gm18) 2'-O-methyltransferase, tRNA (Gm18) methyltransferase, tRNA (guanosine-2'-O-)-methyltransferase, tRNA Gm18 methyltransferase, tRNA guanosine 2'-methyltransferase
ECTree
Advanced search results
Engineering
Engineering on EC 2.1.1.34 - tRNA (guanosine18-2'-O)-methyltransferase
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E124A
H71A
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has increased affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
K32A
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no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
K90A
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no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
L179Stop
N152A
N35D
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marked decrease in Km-value for tRNA, low affinity for S-adenosyl-L-homocysteine
R109A
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no change of affinity for S-adenosyl-L-methionine and slightly increased affinity for tRNA
R11A
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has lost its affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R14M
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dissociation of subunits consistent with that from the wild-type enzyme
R166A
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no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R168A
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no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R176A
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no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R19A
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no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R8A
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no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R14M
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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dissociation of subunits consistent with that from the wild-type enzyme
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additional information
E124A
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extensive structural alterations compared to wild-type, marked decrease in activity
L179Stop
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no change of affinity for S-adenosyl-L-methionine, markedly decreased affinity for tRNA
N152A
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extensive structural alterations compared to wild-type, marked decrease in activity
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spoU gene mutant contains no residue 18, shows no activity but does not influence growth rate
additional information
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chimeric proteins of Escherichia coli and Thermus thermophilus enzymes demonstrate that the catalytic domain discriminates substrate tRNAs from nonsubstrate tRNAs. The N- and C-terminal regions do not function in the substrate tRNA discrimination process. The C-terminal region works in the initial binding process, in which nonsubstrate tRNA is not excluded, and structural movement of the motif 2 region of the catalytic domain in an induced-fit process is involved in substrate tRNA discrimination
additional information
Q9FAC4
chimeric proteins of Escherichia coli and Thermus thermophilus enzymes demonstrate that the catalytic domain discriminates substrate tRNAs from nonsubstrate tRNAs. The N- and C-terminal regions do not function in the substrate tRNA discrimination process. The C-terminal region works in the initial binding process, in which nonsubstrate tRNA is not excluded, and structural movement of the motif 2 region of the catalytic domain in an induced-fit process is involved in substrate tRNA discrimination
additional information
-
chimeric proteins of Escherichia coli and Thermus thermophilus enzymes demonstrate that the catalytic domain discriminates substrate tRNAs from nonsubstrate tRNAs. The N- and C-terminal regions do not function in the substrate tRNA discrimination process. The C-terminal region works in the initial binding process, in which nonsubstrate tRNA is not excluded, and structural movement of the motif 2 region of the catalytic domain in an induced-fit process is involved in substrate tRNA discrimination