Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.4.3.2 extracted from

  • Park, J.H.; Johansson, H.E.; Aoki, H.; Huang, B.X.; Kim, H.Y.; Ganoza, M.C.; Park, M.H.
    Post-translational modification by beta-lysylation is required for activity of Escherichia coli elongation factor P (EF-P) (2012), J. Biol. Chem., 287, 2579-2590.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.3.2

Cloned(Commentary)

Cloned (Comment) Organism
gene yjeK, construction of polycistronic vectors encoding His-tagged or non-tagged EF-P, with YjeA, a class II lysyl-tRNA synthetase, and YjeK and overexpression in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information enzyme knockout mutant generation, phenotype, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Escherichia coli lysyl modification at lysine 34 in native and recombinant bacterial elongation factor-P proteins, no activity with bacterial elongation factor-P mutant K34A (3S)-3,6-diaminohexanoate
-
 ?
L-lysine Escherichia coli K-16 lysyl modification at lysine 34 in native and recombinant bacterial elongation factor-P proteins, no activity with bacterial elongation factor-P mutant K34A (3S)-3,6-diaminohexanoate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 MG1655, gene yjeK
-
Escherichia coli K-16
-
 MG1655, gene yjeK
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine
-
 Escherichia coli (3S)-3,6-diaminohexanoate
-
 ?
L-lysine lysyl modification at lysine 34 in native and recombinant bacterial elongation factor-P proteins, no activity with bacterial elongation factor-P mutant K34A Escherichia coli (3S)-3,6-diaminohexanoate
-
 ?
L-lysine
-
 Escherichia coli K-16 (3S)-3,6-diaminohexanoate
-
 ?
L-lysine lysyl modification at lysine 34 in native and recombinant bacterial elongation factor-P proteins, no activity with bacterial elongation factor-P mutant K34A Escherichia coli K-16 (3S)-3,6-diaminohexanoate
-
 ?

Synonyms

Synonyms Comment Organism
YjeK
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function class II lysyl-tRNA synthetase and lysine-2,3-aminomutase are implicated in the modification of bacterial elongation factor P, EF-P, to convert a specific lysine to a hypothetical beta-lysyl-lysine. Both enzymes, YjeA and YjeK, are required forbeta-lysylation of EF-P. beta-Lysyl-EF-P stimulated N-formyl-methionyl-puromycin synthesis 4fold over the preparations containing unmodified EF-P and/or beta-lysyl-EF-P. The mutant K34A lacking the modification site lysine is inactive. YjeA canbeta-lysylate EF-P in vitro or in cells independently of YjeK. In contrast, YjeK alone or supplementation with D-beta-lysine cannot lysylate EF-P Escherichia coli