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Literature summary for 2.3.2.20 extracted from

  • Sauguet, L.; Moutiez, M.; Li, Y.; Belin, P.; Seguin, J.; Le Du, M.H.; Thai, R.; Masson, C.; Fonvielle, M.; Pernodet, J.L.; Charbonnier, J.B.; Gondry, M.
    Cyclodipeptide synthases, a family of class-I aminoacyl-tRNA synthetase-like enzymes involved in non-ribosomal peptide synthesis (2011), Nucleic Acids Res., 39, 4475-4489.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Streptomyces noursei

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.9 A resolution, monomer that presents a compact alpha/beta structure. It is composed of a central beta-sheet with five parallel beta strands surrounded by ten alpha helices. AlbC contains a deep pocket, highly conserved among cyclodipeptide synthases. This pocket accommodates the aminoacyl moiety of the aa-tRNA substrate Streptomyces noursei

Protein Variants

Protein Variants Comment Organism
E182A mutation in putative catalytic pocket, inactive Streptomyces noursei
E182D mutation in putative catalytic pocket, about 1% of wild-type activity Streptomyces noursei
E182Q mutation in putative catalytic pocket, inactive Streptomyces noursei
F59A about 10% of wild-type activity Streptomyces noursei
G35A mutation in putative catalytic pocket, about 5% of wild-type activity Streptomyces noursei
G79A about 70% of wild-type activity Streptomyces noursei
H31A inactive Streptomyces noursei
L200N mutation in putative catalytic pocket Streptomyces noursei
L33Y/L185D mutation in putative catalytic pocket, inactive Streptomyces noursei
P184A about 40% of wild-type activity Streptomyces noursei
S37A mutation in putative catalytic pocket, inactive Streptomyces noursei
S37C mutation in putative catalytic pocket, about 5% of wild-type activity Streptomyces noursei
W54A inactive Streptomyces noursei
Y128A inactive Streptomyces noursei
Y178A mutation in putative catalytic pocket, inactive Streptomyces noursei
Y178F mutation in putative catalytic pocket, about 10% of wild-type activity Streptomyces noursei
Y202A mutation in putative catalytic pocket Streptomyces noursei
Y202F mutation in putative catalytic pocket, about 15% of wild-type activity Streptomyces noursei

Organism

Organism UniProt Comment Textmining
Streptomyces noursei Q8GED7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Streptomyces noursei

Reaction

Reaction Comment Organism Reaction ID
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe = tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl) ping-pong mechanism with a covalent intermediate in which L-Phe is transferred from Phe-tRNA(Phe) to an active serine Streptomyces noursei

Synonyms

Synonyms Comment Organism
AlbC
-
Streptomyces noursei
CDPS
-
Streptomyces noursei
cyclodipeptide synthase
-
Streptomyces noursei