Literature summary extracted from

Hou, Y.M.; Masuda, I.
Kinetic analysis of tRNA methyltransferases (2015), Methods Enzymol., 560, 91-116 .

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
2.1.1.228	additional information	-	additional information	pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays	Methanocaldococcus jannaschii
2.1.1.228	additional information	-	additional information	pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays	Haemophilus influenzae
2.1.1.228	additional information	-	additional information	pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays	Escherichia coli
2.1.1.228	additional information	-	additional information	pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays	Homo sapiens

Metals/Ions

EC Number	Metals/Ions	Comment	Organism
2.1.1.228	Mg2+	required	Methanocaldococcus jannaschii
2.1.1.228	Mg2+	required	Haemophilus influenzae
2.1.1.228	Mg2+	required	Escherichia coli
2.1.1.228	Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Methanocaldococcus jannaschii	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Haemophilus influenzae	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Escherichia coli	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Homo sapiens	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Methanocaldococcus jannaschii NBRC 100440	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Haemophilus influenzae RD	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Methanocaldococcus jannaschii DSM 2661	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Methanocaldococcus jannaschii ATCC 43067	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Methanocaldococcus jannaschii JAL-1	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Haemophilus influenzae DSM 11121	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Haemophilus influenzae KW20	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Haemophilus influenzae ATCC 51907	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	Methanocaldococcus jannaschii JCM 10045	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.1.228	Escherichia coli	P0A873	-	-
2.1.1.228	Haemophilus influenzae	P43912	-	-
2.1.1.228	Haemophilus influenzae ATCC 51907	P43912	-	-
2.1.1.228	Haemophilus influenzae DSM 11121	P43912	-	-
2.1.1.228	Haemophilus influenzae KW20	P43912	-	-
2.1.1.228	Haemophilus influenzae RD	P43912	-	-
2.1.1.228	Homo sapiens	Q32P41	-	-
2.1.1.228	Methanocaldococcus jannaschii	Q58293	i.e. Methanococcus jannaschii	-
2.1.1.228	Methanocaldococcus jannaschii ATCC 43067	Q58293	i.e. Methanococcus jannaschii	-
2.1.1.228	Methanocaldococcus jannaschii DSM 2661	Q58293	i.e. Methanococcus jannaschii	-
2.1.1.228	Methanocaldococcus jannaschii JAL-1	Q58293	i.e. Methanococcus jannaschii	-
2.1.1.228	Methanocaldococcus jannaschii JCM 10045	Q58293	i.e. Methanococcus jannaschii	-
2.1.1.228	Methanocaldococcus jannaschii NBRC 100440	Q58293	i.e. Methanococcus jannaschii	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product	Methanocaldococcus jannaschii	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product	Homo sapiens	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer	Haemophilus influenzae	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer	Escherichia coli	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product	Methanocaldococcus jannaschii NBRC 100440	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer	Haemophilus influenzae RD	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product	Methanocaldococcus jannaschii DSM 2661	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product	Methanocaldococcus jannaschii ATCC 43067	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product	Methanocaldococcus jannaschii JAL-1	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer	Haemophilus influenzae DSM 11121	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer	Haemophilus influenzae KW20	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer	Haemophilus influenzae ATCC 51907	?	-	-
2.1.1.228	additional information	radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product	Methanocaldococcus jannaschii JCM 10045	?	-	-
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Methanocaldococcus jannaschii	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Haemophilus influenzae	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Escherichia coli	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Homo sapiens	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Methanocaldococcus jannaschii NBRC 100440	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Haemophilus influenzae RD	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Methanocaldococcus jannaschii DSM 2661	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Methanocaldococcus jannaschii ATCC 43067	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Methanocaldococcus jannaschii JAL-1	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Haemophilus influenzae DSM 11121	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Haemophilus influenzae KW20	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Haemophilus influenzae ATCC 51907	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
2.1.1.228	S-adenosyl-L-methionine + guanine37 in tRNA	-	Methanocaldococcus jannaschii JCM 10045	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
2.1.1.228	EcTrmD	-	Escherichia coli
2.1.1.228	HiTrmD	-	Haemophilus influenzae
2.1.1.228	HsTrm5	-	Homo sapiens
2.1.1.228	MjTrm5	-	Methanocaldococcus jannaschii
2.1.1.228	TRM5	-	Methanocaldococcus jannaschii
2.1.1.228	TRM5	-	Homo sapiens
2.1.1.228	TrmD	-	Haemophilus influenzae
2.1.1.228	TrmD	-	Escherichia coli
2.1.1.228	TRMT5	-	Homo sapiens
2.1.1.228	tRNA methyltransferase	-	Methanocaldococcus jannaschii
2.1.1.228	tRNA methyltransferase	-	Haemophilus influenzae
2.1.1.228	tRNA methyltransferase	-	Escherichia coli
2.1.1.228	tRNA methyltransferase	-	Homo sapiens

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.1.1.228	37	-	assay at	Haemophilus influenzae
2.1.1.228	37	-	assay at	Escherichia coli
2.1.1.228	37	-	assay at	Homo sapiens
2.1.1.228	55	-	assay at	Methanocaldococcus jannaschii

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
2.1.1.228	8	-	assay at	Methanocaldococcus jannaschii
2.1.1.228	8	-	assay at	Haemophilus influenzae
2.1.1.228	8	-	assay at	Escherichia coli
2.1.1.228	8	-	assay at	Homo sapiens

Cofactor

EC Number	Cofactor	Comment	Organism
2.1.1.228	S-adenosyl-L-methionine	-	Methanocaldococcus jannaschii
2.1.1.228	S-adenosyl-L-methionine	-	Haemophilus influenzae
2.1.1.228	S-adenosyl-L-methionine	-	Escherichia coli
2.1.1.228	S-adenosyl-L-methionine	-	Homo sapiens

General Information

EC Number	General Information	Comment	Organism
2.1.1.228	evolution	at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. Methanococcus jannaschii MjTrm5 is homologous to human Trm5	Homo sapiens
2.1.1.228	evolution	at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. MjTrm5 is homologous to human Trm5	Methanocaldococcus jannaschii
2.1.1.228	evolution	at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. EcTrmD is homologous to Haemophilus influenza TrmD	Escherichia coli
2.1.1.228	evolution	at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. Escherichia coli EcTrmD is homologous to Haemophilus influenza TrmD	Haemophilus influenzae
2.1.1.228	additional information	evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview	Methanocaldococcus jannaschii
2.1.1.228	additional information	evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview	Haemophilus influenzae
2.1.1.228	additional information	evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview	Escherichia coli
2.1.1.228	additional information	evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview	Homo sapiens
2.1.1.228	physiological function	methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome	Methanocaldococcus jannaschii
2.1.1.228	physiological function	methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome	Haemophilus influenzae
2.1.1.228	physiological function	methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome	Escherichia coli
2.1.1.228	physiological function	methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome	Homo sapiens