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2.3.2.20: cyclo(L-leucyl-L-phenylalanyl) synthase

This is an abbreviated version!
For detailed information about cyclo(L-leucyl-L-phenylalanyl) synthase, go to the full flat file.

Word Map on EC 2.3.2.20

Reaction

L-leucyl-tRNALeu
+
L-phenylalanyl-tRNAPhe
=
tRNALeu
 +
tRNAPhe
 +
cyclo(L-leucyl-L-phenylalanyl)

Synonyms

AlbC, BcmA, CDP, CDPS, CDPS 22, CDPS39, cFL synthase, cyclodipeptide synthase, cyclodipeptide synthases, Fdum-CDPS, Nbra-CDPS, NcdA, NCTC11370_02388, Ndas_1148, NozA, O3I_025450, Rgry-CDPS, RICGR_0139

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.20 cyclo(L-leucyl-L-phenylalanyl) synthase

Crystallization

Crystallization on EC 2.3.2.20 - cyclo(L-leucyl-L-phenylalanyl) synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, crystallization from 11% PEG 3350, 0.1 M HEPES, pH 7.5, and 0.2 M L-Pro, X-ray difffraction structure determination and analysis at 3.06 A resolution
purified recombinant enzyme, crystallization from 22% PEG 3350, 0.2 M tri-ammonium citrate, pH 7.0, X-ray difffraction structure determination and analysis at 3.18 A resolution
purified recombinant enzyme, crystallization from 15.2% PEG 3350, 0.1 M potassium fluoride, X-ray difffraction structure determination and analysis at 1.99 A resolution
hanging drop vapor diffusion method, using 10% (w/v) PEG8000, 50 mM KCl, 50 mM sodium cacodylate, pH 6.0
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