BRENDA - Enzyme Database
show all sequences of 2.1.1.228

TrmD A methyl transferase for tRNA methylation with m1G37

Hou, Y.; Matsubara, R.; Takase, R.; Masuda, I.; Sulkowska, J.; Enzymes 41, 89-115 (2017) View publication on PubMedView publication on EuropePMC

Data extracted from this reference:

Application
Application
Commentary
Organism
drug development
TrmD is ranked as a high-priority antimicrobial target
Aquifex aeolicus
drug development
TrmD is ranked as a high-priority antimicrobial target
Escherichia coli
drug development
TrmD is ranked as a high-priority antimicrobial target
Salmonella enterica subsp. enterica serovar Typhimurium
drug development
TrmD is ranked as a high-priority antimicrobial target
Haemophilus influenzae
Cloned(Commentary)
Cloned (Commentary)
Organism
gene trmD, sequence comparisons
Aquifex aeolicus
gene trmD, sequence comparisons
Escherichia coli
gene trmD, sequence comparisons
Salmonella enterica subsp. enterica serovar Typhimurium
gene trmD, sequence comparisons
Haemophilus influenzae
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
can substitute Mg2+ to lesser extent
Aquifex aeolicus
Ca2+
can substitute Mg2+ to lesser extent
Escherichia coli
Ca2+
can substitute Mg2+ to lesser extent
Salmonella enterica subsp. enterica serovar Typhimurium
Ca2+
can substitute Mg2+ to lesser extent
Haemophilus influenzae
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Aquifex aeolicus
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Escherichia coli
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Salmonella enterica subsp. enterica serovar Typhimurium
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Haemophilus influenzae
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
Aquifex aeolicus
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
Escherichia coli
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
Salmonella enterica subsp. enterica serovar Typhimurium
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
Haemophilus influenzae
Ni2+
can substitute Mg2+ to lesser extent
Aquifex aeolicus
Ni2+
can substitute Mg2+ to lesser extent
Escherichia coli
Ni2+
can substitute Mg2+ to lesser extent
Salmonella enterica subsp. enterica serovar Typhimurium
Ni2+
can substitute Mg2+ to lesser extent
Haemophilus influenzae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Aquifex aeolicus
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Escherichia coli
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Salmonella enterica subsp. enterica serovar Typhimurium
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Haemophilus influenzae
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
S-adenosyl-L-methionine + guanine37 in tRNA
Aquifex aeolicus
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Escherichia coli
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Salmonella enterica subsp. enterica serovar Typhimurium
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Haemophilus influenzae
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Aquifex aeolicus
O67463
-
-
Escherichia coli
P0A873
-
-
Haemophilus influenzae
A0A0D0GZF5
-
-
Salmonella enterica subsp. enterica serovar Typhimurium
P36245
-
-
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
P36245
-
-
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
P36245
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Aquifex aeolicus
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Escherichia coli
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Salmonella enterica subsp. enterica serovar Typhimurium
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Haemophilus influenzae
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
?
-
-
-
-
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Aquifex aeolicus
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Escherichia coli
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Salmonella enterica subsp. enterica serovar Typhimurium
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Haemophilus influenzae
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
TrmD is an obligated homodimer that places each active site at the dimer interface
Aquifex aeolicus
dimer
TrmD is an obligated homodimer that places each active site at the dimer interface
Escherichia coli
dimer
TrmD is an obligated homodimer that places each active site at the dimer interface
Salmonella enterica subsp. enterica serovar Typhimurium
dimer
TrmD is an obligated homodimer that places each active site at the dimer interface
Haemophilus influenzae
More
in both monomeric chains of TrmD, AdoMet is bound in the N-terminal domain to the deep cleft of a trefoil knot fold, which is a topological knot that involves three crossings of the protein backbone through a loop, the trefoil knot in TrmD is shown to be required for methyl transfer, knot structure and function, overview. The trefoil knot of TrmD is required for the catalytic mechanism in three ways
Escherichia coli
More
in both monomeric chains of TrmD, AdoMet is bound in the N-terminal domain to the deep cleft of a trefoil knot fold, which is a topological knot that involves three crossings of the protein backbone through a loop, the trefoil knot in TrmD is shown to be required for methyl transfer, knot structure and function, overview. The trefoil knot of TrmD is required for the catalytic mechanism in three ways
Salmonella enterica subsp. enterica serovar Typhimurium
More
in both monomeric chains of TrmD, AdoMet is bound in the N-terminal domain to the deep cleft of a trefoil knot fold, which is a topological knot that involves three crossings of the protein backbone through a loop, the trefoil knot in TrmD is shown to be required for methyl transfer, knot structure and function, overview. The trefoil knot of TrmD is required for the catalytic mechanism in three ways
Haemophilus influenzae
More
without the knot, as found in the crystal structure of Aquifex aeolicus TrmD, AdoMet cannot bend and can only exist in the open shape. Without being in the bent shape, AdoMet is be positioned in a spatial geometry incompatible with the position of the G37 base and unfavorable for methyl transfer. The m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA
Aquifex aeolicus
Synonyms
Synonyms
Commentary
Organism
EcTrmD
-
Escherichia coli
HiTrmD
-
Haemophilus influenzae
TrmD
-
Aquifex aeolicus
TrmD
-
Escherichia coli
TrmD
-
Salmonella enterica subsp. enterica serovar Typhimurium
TrmD
-
Haemophilus influenzae
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Aquifex aeolicus
S-adenosyl-L-methionine
-
Escherichia coli
S-adenosyl-L-methionine
-
Salmonella enterica subsp. enterica serovar Typhimurium
S-adenosyl-L-methionine
-
Haemophilus influenzae
Application (protein specific)
Application
Commentary
Organism
drug development
TrmD is ranked as a high-priority antimicrobial target
Aquifex aeolicus
drug development
TrmD is ranked as a high-priority antimicrobial target
Escherichia coli
drug development
TrmD is ranked as a high-priority antimicrobial target
Salmonella enterica subsp. enterica serovar Typhimurium
drug development
TrmD is ranked as a high-priority antimicrobial target
Haemophilus influenzae
Cloned(Commentary) (protein specific)
Commentary
Organism
gene trmD, sequence comparisons
Aquifex aeolicus
gene trmD, sequence comparisons
Escherichia coli
gene trmD, sequence comparisons
Salmonella enterica subsp. enterica serovar Typhimurium
gene trmD, sequence comparisons
Haemophilus influenzae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Aquifex aeolicus
S-adenosyl-L-methionine
-
Escherichia coli
S-adenosyl-L-methionine
-
Salmonella enterica subsp. enterica serovar Typhimurium
S-adenosyl-L-methionine
-
Haemophilus influenzae
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
can substitute Mg2+ to lesser extent
Aquifex aeolicus
Ca2+
can substitute Mg2+ to lesser extent
Escherichia coli
Ca2+
can substitute Mg2+ to lesser extent
Salmonella enterica subsp. enterica serovar Typhimurium
Ca2+
can substitute Mg2+ to lesser extent
Haemophilus influenzae
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Aquifex aeolicus
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Escherichia coli
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Salmonella enterica subsp. enterica serovar Typhimurium
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Haemophilus influenzae
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
Aquifex aeolicus
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
Escherichia coli
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
Salmonella enterica subsp. enterica serovar Typhimurium
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
Haemophilus influenzae
Ni2+
can substitute Mg2+ to lesser extent
Aquifex aeolicus
Ni2+
can substitute Mg2+ to lesser extent
Escherichia coli
Ni2+
can substitute Mg2+ to lesser extent
Salmonella enterica subsp. enterica serovar Typhimurium
Ni2+
can substitute Mg2+ to lesser extent
Haemophilus influenzae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Aquifex aeolicus
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Escherichia coli
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Salmonella enterica subsp. enterica serovar Typhimurium
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Haemophilus influenzae
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
additional information
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
?
-
-
-
S-adenosyl-L-methionine + guanine37 in tRNA
Aquifex aeolicus
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Escherichia coli
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Salmonella enterica subsp. enterica serovar Typhimurium
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Haemophilus influenzae
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Aquifex aeolicus
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Escherichia coli
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Salmonella enterica subsp. enterica serovar Typhimurium
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Haemophilus influenzae
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
?
-
-
-
-
additional information
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
756631
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
?
-
-
-
-
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Aquifex aeolicus
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Escherichia coli
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Salmonella enterica subsp. enterica serovar Typhimurium
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Haemophilus influenzae
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
-
756631
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
TrmD is an obligated homodimer that places each active site at the dimer interface
Aquifex aeolicus
dimer
TrmD is an obligated homodimer that places each active site at the dimer interface
Escherichia coli
dimer
TrmD is an obligated homodimer that places each active site at the dimer interface
Salmonella enterica subsp. enterica serovar Typhimurium
dimer
TrmD is an obligated homodimer that places each active site at the dimer interface
Haemophilus influenzae
More
in both monomeric chains of TrmD, AdoMet is bound in the N-terminal domain to the deep cleft of a trefoil knot fold, which is a topological knot that involves three crossings of the protein backbone through a loop, the trefoil knot in TrmD is shown to be required for methyl transfer, knot structure and function, overview. The trefoil knot of TrmD is required for the catalytic mechanism in three ways
Escherichia coli
More
in both monomeric chains of TrmD, AdoMet is bound in the N-terminal domain to the deep cleft of a trefoil knot fold, which is a topological knot that involves three crossings of the protein backbone through a loop, the trefoil knot in TrmD is shown to be required for methyl transfer, knot structure and function, overview. The trefoil knot of TrmD is required for the catalytic mechanism in three ways
Salmonella enterica subsp. enterica serovar Typhimurium
More
in both monomeric chains of TrmD, AdoMet is bound in the N-terminal domain to the deep cleft of a trefoil knot fold, which is a topological knot that involves three crossings of the protein backbone through a loop, the trefoil knot in TrmD is shown to be required for methyl transfer, knot structure and function, overview. The trefoil knot of TrmD is required for the catalytic mechanism in three ways
Haemophilus influenzae
More
without the knot, as found in the crystal structure of Aquifex aeolicus TrmD, AdoMet cannot bend and can only exist in the open shape. Without being in the bent shape, AdoMet is be positioned in a spatial geometry incompatible with the position of the G37 base and unfavorable for methyl transfer. The m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA
Aquifex aeolicus
General Information
General Information
Commentary
Organism
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species
Aquifex aeolicus
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species
Salmonella enterica subsp. enterica serovar Typhimurium
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species. In all of the available structures of the TrmD dimer, each monomeric chain is made up of three distinct domains: an N-terminal domain (residues 1-160 in HiTrmD and EcTrmD) for binding AdoMet, a C-terminal domain for binding tRNA (residues 169-246), and a flexible linker in between (residues 161-168)
Escherichia coli
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species. In all of the available structures of the TrmD dimer, each monomeric chain is made up of three distinct domains: an N-terminal domain (residues 1-160 in HiTrmD and EcTrmD) for binding AdoMet, a C-terminal domain for binding tRNA (residues 169-246), and a flexible linker in between (residues 161-168)
Haemophilus influenzae
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
Aquifex aeolicus
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
Escherichia coli
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
Salmonella enterica subsp. enterica serovar Typhimurium
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
Haemophilus influenzae
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
Aquifex aeolicus
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
Escherichia coli
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
Salmonella enterica subsp. enterica serovar Typhimurium
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
Haemophilus influenzae
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. The methylated m1G37 is on the 3?-side of the anticodon, and it is necessary for suppressing tRNA frameshifting during protein synthesis on the ribosome TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The Mg2+ dependence is important for regulating Mg2+ transport to Salmonella for survival of the pathogen in the host cell. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
Salmonella enterica subsp. enterica serovar Typhimurium
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism
Aquifex aeolicus
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
Escherichia coli
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
Haemophilus influenzae
General Information (protein specific)
General Information
Commentary
Organism
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species
Aquifex aeolicus
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species
Salmonella enterica subsp. enterica serovar Typhimurium
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species. In all of the available structures of the TrmD dimer, each monomeric chain is made up of three distinct domains: an N-terminal domain (residues 1-160 in HiTrmD and EcTrmD) for binding AdoMet, a C-terminal domain for binding tRNA (residues 169-246), and a flexible linker in between (residues 161-168)
Escherichia coli
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species. In all of the available structures of the TrmD dimer, each monomeric chain is made up of three distinct domains: an N-terminal domain (residues 1-160 in HiTrmD and EcTrmD) for binding AdoMet, a C-terminal domain for binding tRNA (residues 169-246), and a flexible linker in between (residues 161-168)
Haemophilus influenzae
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
Aquifex aeolicus
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
Escherichia coli
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
Salmonella enterica subsp. enterica serovar Typhimurium
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
Haemophilus influenzae
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
Aquifex aeolicus
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
Escherichia coli
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
Salmonella enterica subsp. enterica serovar Typhimurium
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
Haemophilus influenzae
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. The methylated m1G37 is on the 3?-side of the anticodon, and it is necessary for suppressing tRNA frameshifting during protein synthesis on the ribosome TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The Mg2+ dependence is important for regulating Mg2+ transport to Salmonella for survival of the pathogen in the host cell. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
Salmonella enterica subsp. enterica serovar Typhimurium
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism
Aquifex aeolicus
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
Escherichia coli
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
Haemophilus influenzae
Other publictions for EC 2.1.1.228
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Protein Variants
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
kcat/KM [mM/s]
kcat/KM [mM/s] (protein specific)
755697
Zhong
Targeting the bacterial epitr ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14
ACS Infect. Dis.
5
326-335
2019
-
1
1
-
-
-
63
2
-
-
-
2
-
8
-
-
-
-
-
-
-
-
6
-
3
-
-
1
2
-
-
-
1
-
-
63
-
1
1
1
-
-
-
63
63
-
2
-
-
-
2
-
-
-
-
-
-
-
-
6
-
-
-
1
2
-
-
-
-
-
1
1
-
2
2
756152
Li
Backbone resonance assignment ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14
Biomol. NMR Assign.
13
327-332
2019
-
1
1
-
-
-
1
-
-
-
-
2
-
7
-
-
1
-
-
1
-
-
2
2
2
-
-
-
-
1
-
-
1
-
-
-
-
1
1
1
-
-
-
-
1
-
-
-
-
-
2
-
-
-
1
-
1
-
-
2
2
-
-
-
-
1
-
-
-
-
2
2
-
-
-
756153
Li
Backbone resonance assignment ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14
Biomol. NMR Assign.
13
49-53
2019
-
-
1
-
-
-
2
-
-
-
-
2
-
6
-
-
1
-
-
-
-
-
2
-
2
-
-
1
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
2
-
-
-
-
-
2
-
-
-
1
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
756774
Hou
Codon-specific translation by ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720, Saccharomyces cerevisiae ATCC 204508
Front. Genet.
10
713
2019
-
-
-
-
1
-
-
-
-
2
-
7
-
8
-
-
-
-
-
-
-
-
7
-
4
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
2
-
7
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
1
8
8
1
-
-
757408
Whitehouse
Development of inhibitors aga ...
Mycobacteroides abscessus
J. Med. Chem.
62
7210-7232
2019
-
1
1
1
-
-
50
-
-
-
-
1
-
6
-
-
1
-
-
-
-
-
1
1
2
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
1
-
-
-
50
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
757409
Zhong
Thienopyrimidinone derivative ...
Staphylococcus aureus, Mycobacterium tuberculosis, Pseudomonas aeruginosa
J. Med. Chem.
62
7788-7805
2019
-
-
3
2
-
3
42
3
-
2
-
3
-
5
-
-
-
-
-
-
-
-
3
-
12
1
-
-
-
1
-
-
3
-
-
26
-
-
3
3
2
-
3
26
42
-
3
-
2
-
3
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
757863
Jin
AtTrm5a catalyses 1-methylgua ...
Arabidopsis thaliana
Nucleic Acids Res.
47
883-898
2019
-
-
1
-
1
-
-
-
1
1
-
2
-
8
-
-
1
-
-
2
-
-
2
-
3
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
1
1
-
2
-
-
-
1
-
2
-
-
2
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
758329
Jaroensuk
Crystal structure and catalyt ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14
RNA
25
1481-1496
2019
-
1
1
1
1
-
1
3
-
2
-
2
-
10
-
-
1
-
-
-
-
-
14
2
5
1
-
-
2
1
-
-
1
3
-
-
-
1
1
1
1
1
-
-
1
3
3
-
2
-
2
-
-
-
1
-
-
-
-
14
2
1
-
-
2
1
-
-
-
-
2
2
-
2
2
757201
Zhou
A hypertension-associated mit ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii NBRC 100440, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii ATCC 43067, Methanocaldococcus jannaschii JAL-1, Methanocaldococcus jannaschii JCM 10045
J. Biol. Chem.
293
1425-1438
2018
-
-
-
-
1
-
-
-
-
-
-
6
-
17
-
-
-
-
-
-
-
-
12
-
5
-
-
-
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1
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1
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6
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12
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1
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756161
Goto-Ito
Trm5 and TrmD two enzymes fr ...
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30
4
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14
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756163
Hori
Transfer RNA methyltransferas ...
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3
3
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3
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3
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3
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6
3
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7
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756631
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TrmD A methyl transferase fo ...
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758348
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758324
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TRMT5 mutations cause a defect ...
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757582
Hou
Kinetic analysis of tRNA meth ...
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729858
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Transfer RNA methyltransferase ...
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737226
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737228
Paris
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Sakaguchi
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18
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2012
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2
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10
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721029
Lahoud
Differentiating analogous tRNA ...
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RNA
17
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2011
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2
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721026
Christian
Mechanism of N-methylation by ...
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16
2484-2492
2010
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1
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701123
Goto-Ito
Crystal structure of archaeal ...
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1
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Toyooka
Stabilization of tRNA (mG37) m ...
Aquifex aeolicus
Genes Cells
13
807-816
2008
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1
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Yeast mitochondrial initiator ...
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Catalysis by the second class ...
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11
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661154
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20
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662010
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