Literature summary for 2.1.1.228 extracted from

Christian, T.; Lahoud, G.; Liu, C.; Hoffmann, K.; Perona, J.J.; Hou, Y.M.
Mechanism of N-methylation by the tRNA m1G37 methyltransferase Trm5 (2010), RNA, 16, 2484-2492.

Search for more literature for 2.1.1.228

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of the crystal structure of the Trm5-tRNA-AdoMet ternary complex	Methanocaldococcus jannaschii

Protein Variants

Protein Variants	Comment	Organism
D223A	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
D223E	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
D223L	site-directed mutagenesis, the mutant shows complete loss of activity	Methanocaldococcus jannaschii
D223N	site-directed mutagenesis, the mutant shows complete loss of activity	Methanocaldococcus jannaschii
E185A	site-directed mutagenesis, the mutant shows complete loss of activity	Methanocaldococcus jannaschii
E185D	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
E185Q	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
K137A	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
K318A	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
N265A	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
N265H	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
N265Q	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
P267A	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
R145A	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
R181A	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
R186A	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
Y177A	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii
Y177F	site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme	Methanocaldococcus jannaschii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	wild-type and mutant enzymes pH-dependence of the single-turnover rate constant: the pH dependence of kobs in single-turnover analysis corresponds to proton ransfer during a slower process of induced fit, rather than the bond-breaking and bond-forming steps of methyl transfer, detailed analysis and overview	Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + guanine37 in tRNA	Methanocaldococcus jannaschii	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?

Organism

Organism	UniProt	Comment	Textmining
Methanocaldococcus jannaschii	Q58293	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	mechanism of N-methylation by the tRNA m1G37 methyltransferase Trm5 involving proton abstraction during docking of G37 in the active site by a general base , E185	Methanocaldococcus jannaschii	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	85°C is the optimal growth temperature	Methanocaldococcus jannaschii	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	structure of Trm5 active site bound to tRNA and S-adenosyl-L-methionine, induced fit for active-site assembly, detailed overview. E185 is crucial both for general base catalysis and for the conformational change that precedes catalysis	Methanocaldococcus jannaschii	?	-	?
S-adenosyl-L-methionine + guanine37 in tRNA	-	Methanocaldococcus jannaschii	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
S-adenosyl-L-methionine + guanine37 in tRNACys	Methanococcus jannaschii tRNACys	Methanocaldococcus jannaschii	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys	-	?

Synonyms

Synonyms	Comment	Organism
TRM5	-	Methanocaldococcus jannaschii
tRNA m1G37 methyltransferase	-	Methanocaldococcus jannaschii

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
55	-	assay at	Methanocaldococcus jannaschii

pH Range

pH Minimum	pH Maximum	Comment	Organism
6	9.8	preincubation of Trm5 at pH 6.0, followed by adjustment of the solution to pH 8.0, does not cause irreversible inactivation of the enzyme. Enzyme treated in this manner retained equivalent activity in single-turnover assay	Methanocaldococcus jannaschii

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	-	Methanocaldococcus jannaschii

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Release 2023.1 (January 2023)