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Literature summary for 2.1.1.35 extracted from

  • Gustafsson, C.; Björk, G.R.
    The tRNA-(m5U54)-methyltransferase of Escherichia coli is present in two forms in vivo, one of which is present as bound to tRNA and to a 3-end fragment of 16S rRNA (1993), J. Biol. Chem., 268, 1326-1331.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
trmA gene encodes enzyme, gene is essential for the organism Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
native enzyme form, sucrose density gradient centrifugation Escherichia coli
54000
-
TrmA/RNA complex, sucrose density gradient centrifugation Escherichia coli
62000
-
x * 54000, first TrmA/RNA-complex, x * 62000, second TrmA/RNA-complex, x * 42000, native enzyme form, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + uridine54 in tRNA Escherichia coli in vivo present both as 42 kDa polypeptide and as covalent TrmA/RNA complex, to equal amounts, both with methylating activity, in vivo the m5U54 modification confers a small selective growth advantage, two different catalytic activities: synthesis of m5U54 and an unknown essential function, may be associated with binding RNA, either during a maturation process of the rRNA and/or tRNA or as a regulatory device during the assembly and maturation of the translational apparatus such as an RNA chaperone S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
?
S-adenosyl-L-methionine + uridine54 in tRNA Escherichia coli 1100 in vivo present both as 42 kDa polypeptide and as covalent TrmA/RNA complex, to equal amounts, both with methylating activity, in vivo the m5U54 modification confers a small selective growth advantage, two different catalytic activities: synthesis of m5U54 and an unknown essential function, may be associated with binding RNA, either during a maturation process of the rRNA and/or tRNA or as a regulatory device during the assembly and maturation of the translational apparatus such as an RNA chaperone S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli
-
3 enzyme forms: native protein and 2 different TrmA/RNA complexes
-
Escherichia coli 1100
-
-
-

Purification (Commentary)

Purification (Comment) Organism
3 enzyme forms Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + uracil54 in tRNA = S-adenosyl-L-homocysteine + 5-methyluracil54 in tRNA catalytic mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme is present as 42 kDa native protein or as 2 different covalent TrmA/RNA complexes, with TrmA as a 54 kDa and a 62 kDa polypeptide, respectively, RNA is a subset of undermodified tRNA species as well as the 3Â’ terminus of 16S rRNA, RNA does not affect enzyme activity Escherichia coli additional information
-
?
additional information enzyme is present as 42 kDa native protein or as 2 different covalent TrmA/RNA complexes, with TrmA as a 54 kDa and a 62 kDa polypeptide, respectively, RNA is a subset of undermodified tRNA species as well as the 3Â’ terminus of 16S rRNA, RNA does not affect enzyme activity Escherichia coli 1100 additional information
-
?
S-adenosyl-L-methionine + uridine54 in tRNA enzyme transfers methyl group to uridine in position 54 of the TPsi-loop of all E. coli tRNA species, requires the TPsi-arm and, most specifically, the bases U54-U55-C56-Pu57-A58 for tRNA recognition Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA formation of 5-methyluridine ?
S-adenosyl-L-methionine + uridine54 in tRNA methyl group acceptor: tRNA from E. coli Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA formation of 5-methyluridine ?
S-adenosyl-L-methionine + uridine54 in tRNA in vivo present both as 42 kDa polypeptide and as covalent TrmA/RNA complex, to equal amounts, both with methylating activity, in vivo the m5U54 modification confers a small selective growth advantage, two different catalytic activities: synthesis of m5U54 and an unknown essential function, may be associated with binding RNA, either during a maturation process of the rRNA and/or tRNA or as a regulatory device during the assembly and maturation of the translational apparatus such as an RNA chaperone Escherichia coli S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
?
S-adenosyl-L-methionine + uridine54 in tRNA enzyme transfers methyl group to uridine in position 54 of the TPsi-loop of all E. coli tRNA species, requires the TPsi-arm and, most specifically, the bases U54-U55-C56-Pu57-A58 for tRNA recognition Escherichia coli 1100 S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA formation of 5-methyluridine ?
S-adenosyl-L-methionine + uridine54 in tRNA methyl group acceptor: tRNA from E. coli Escherichia coli 1100 S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA formation of 5-methyluridine ?
S-adenosyl-L-methionine + uridine54 in tRNA in vivo present both as 42 kDa polypeptide and as covalent TrmA/RNA complex, to equal amounts, both with methylating activity, in vivo the m5U54 modification confers a small selective growth advantage, two different catalytic activities: synthesis of m5U54 and an unknown essential function, may be associated with binding RNA, either during a maturation process of the rRNA and/or tRNA or as a regulatory device during the assembly and maturation of the translational apparatus such as an RNA chaperone Escherichia coli 1100 S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA
-
?

Subunits

Subunits Comment Organism
? x * 54000, first TrmA/RNA-complex, x * 62000, second TrmA/RNA-complex, x * 42000, native enzyme form, SDS-PAGE Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

Cofactor

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