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Literature summary extracted from

  • Christian, T.; Lahoud, G.; Liu, C.; Hou, Y.M.
    Control of catalytic cycle by a pair of analogous tRNA modification enzymes (2010), J. Mol. Biol., 400, 204-217.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.228 additional information
-
 additional information pre-steady-state and steady-state kinetics, rapid burst phase followed by a slower and linear phase in reaction, single-turnover and from steady-state analysis, overview Methanocaldococcus jannaschii
2.1.1.228 additional information
-
 additional information pre-steady-state and steady-state kinetics, time-dependent linear reaction, overview. TrmD exhibits half-of-the-sites reactivity in which only one of the two active sites is functional at a given time Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.228 additional information Methanocaldococcus jannaschii Trm5 catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon ?
-
 ?
2.1.1.228 additional information Escherichia coli TrmD catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon ?
-
 ?
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 Methanocaldococcus jannaschii
-
 S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.228 Escherichia coli
-
-
-
2.1.1.228 Methanocaldococcus jannaschii
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.228 additional information Trm5 catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon Methanocaldococcus jannaschii ?
-
 ?
2.1.1.228 additional information TrmD catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon Escherichia coli ?
-
 ?
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
-
 Methanocaldococcus jannaschii S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA
-
 Methanocaldococcus jannaschii S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA tight binding of Trm5 to products ?
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA substrate binding stoichiometry to TrmD, dissociation constants, overview Escherichia coli S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.228 dimer TrmD features a trefoil-knot active-site structure Escherichia coli
2.1.1.228 More Trm5 features the Rossmann fold Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
2.1.1.228 TRM5
-
 Methanocaldococcus jannaschii
2.1.1.228 TrmD
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.228 additional information
-
 additional information 0.12 is kchem in the first rapid burst turnover Methanocaldococcus jannaschii
2.1.1.228 0.02
-
 S-adenosyl-L-methionine kcat in steady-state phase turnover, pH and temperature not specified in the publication Methanocaldococcus jannaschii
2.1.1.228 0.09
-
 S-adenosyl-L-methionine pH and temperature not specified in the publication Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.228 S-adenosyl-L-methionine
-
 Escherichia coli
2.1.1.228 S-adenosyl-L-methionine
-
 Methanocaldococcus jannaschii