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Literature summary for 2.1.1.228 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
Search for more literature for 2.1.1.228

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Methanocaldococcus jannaschii Trm5 catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon ?
-
 ?
additional information Escherichia coli TrmD catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon ?
-
 ?
S-adenosyl-L-methionine + guanine37 in tRNA Escherichia coli
-
 S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?
S-adenosyl-L-methionine + guanine37 in tRNA Methanocaldococcus jannaschii
-
 S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Methanocaldococcus jannaschii
-
-
-

Substrates and Products (Substrate)

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

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

Synonyms

Synonyms Comment Organism
TRM5
-
 Methanocaldococcus jannaschii
TrmD
-
 Escherichia coli

Turnover Number [1/s]

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

Cofactor

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