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Literature summary for 2.1.1.34 extracted from

  • Ochi, A.; Makabe, K.; Yamagami, R.; Hirata, A.; Sakaguchi, R.; Hou, Y.M.; Watanabe, K.; Nureki, O.; Kuwajima, K.; Hori, H.
    The catalytic domain of topological knot tRNA methyltransferase (TrmH) discriminates between substrate tRNA and nonsubstrate tRNA via an induced-fit process (2013), J. Biol. Chem., 288, 25562-25574.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.34

Cloned(Commentary)

Cloned (Comment) Organism
expression inb Escherichia coli Escherichia coli
expression inb Escherichia coli Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
D180A 42% of wild-type activity Thermus thermophilus
D190A 5% of wild-type activity Thermus thermophilus
E182A 29% of wild-type activity Thermus thermophilus
K186A 7% of wild-type activity Thermus thermophilus
L179Stop complete loss of activity Thermus thermophilus
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 Escherichia coli
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 Thermus thermophilus
Q185A 16% of wild-type activity Thermus thermophilus
V187A 11% of wild-type activity Thermus thermophilus
Y184A 10% of wild-type activity Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00011
-
 guanosine18 in yeast tRNAPhe mutant E182A, pH not specified in the publication, temperature not specified in the publication Thermus thermophilus
0.00012
-
 guanosine18 in yeast tRNAPhe mutant D180A, pH not specified in the publication, temperature not specified in the publication Thermus thermophilus
0.00012
-
 guanosine18 in yeast tRNAPhe mutant Q185A, pH not specified in the publication, temperature not specified in the publication Thermus thermophilus
0.00014
-
 guanosine18 in yeast tRNAPhe mutant V187A, pH not specified in the publication, temperature not specified in the publication Thermus thermophilus
0.00015
-
 guanosine18 in yeast tRNAPhe wild-type, pH not specified in the publication, temperature not specified in the publication Thermus thermophilus
0.00016
-
 guanosine18 in yeast tRNAPhe mutant K186A, pH not specified in the publication, temperature not specified in the publication Thermus thermophilus
0.00026
-
 guanosine18 in yeast tRNAPhe mutant Y184A, pH not specified in the publication, temperature not specified in the publication Thermus thermophilus
0.0013
-
 guanosine18 in yeast tRNAPhe mutant D190A, pH not specified in the publication, temperature not specified in the publication Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Thermus thermophilus Q9FAC4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + guanosine18 in yeast tRNAPhe
-
 Escherichia coli S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNAPhe
-
 ?
S-adenosyl-L-methionine + guanosine18 in yeast tRNAPhe
-
 Thermus thermophilus S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNAPhe
-
 ?

Synonyms

Synonyms Comment Organism
tRNA (Gm18) methyltransferase
-
 Escherichia coli
tRNA (Gm18) methyltransferase
-
 Thermus thermophilus