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Literature summary extracted from

  • Van Noort, J.M.; Kraal, B.; Sinjorgo, K.M.; Persoon, N.L.M.; Johanns, E.S.D.; Bosch, L.
    Methylation in vivo of elongation factor EF-Tu at lysine-56 decreases the rate of tRNA-dependent GTP hydrolysis (1986), Eur. J. Biochem., 160, 557-561.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.6.5.3 medicine protein biosynthesis Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.5.3 GTP + H2O Escherichia coli
-
GDP + phosphate
-
?
3.6.5.3 guanosine 5'-(thio)triphosphate + H2O Escherichia coli
-
GDP + thiophosphate + 3 H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.6.5.3 Escherichia coli
-
elongations factor (EF)Tu
-
3.6.5.3 Escherichia coli
-
strains MRE600, unmethylated enzyme, and LBE 1001, methylated enzyme
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.6.5.3 side-chain modification methylation of lysine-56, enzyme with decreased rate of tRNA-dependent GTP hydrolysis Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.5.3
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.5.3 GTP + H2O
-
Escherichia coli GDP + phosphate
-
?
3.6.5.3 guanosine 5'-(thio)triphosphate + H2O
-
Escherichia coli GDP + thiophosphate + 3 H+
-
?