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1.14.20.1: deacetoxycephalosporin-C synthase

This is an abbreviated version!
For detailed information about deacetoxycephalosporin-C synthase, go to the full flat file.

Word Map on EC 1.14.20.1

Reaction

Penicillin N
+
2-oxoglutarate
 +
O2
=
deacetoxycephalosporin C
 +
succinate
 +
CO2
 +
H2O

Synonyms

acDAOC/DACS, cefE, cefEF, Cephalosporin biosynthesis expandase/hydroxylase, DAOC synthase, DAOC/DAC synthase, DAOC/DACS, DAOCS, deacetoxy/deacetylcephalosporin C synthase, deacetoxycephalosporin C synthase, deacetoxycephalosporin-C synthase, deacetoxycephalosporin-C synthetase, deacetoxycephalosporin/deacetylcephalosporin C synthase, expandase, expendase, penicillin N expandase, scDAOCS

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated
                1.14.20.1 deacetoxycephalosporin-C synthase

Crystallization

Crystallization on EC 1.14.20.1 - deacetoxycephalosporin-C synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the DAOC synthase is in trimeric form, C-terminal end of the protein is responsible for the oligomerization process, addition of Fe2+ or 2-oxoglutarate shifts the equilibrium toward the monomeric form that appears to be the active form in solution
-
as apoprotein with N-terminal His tag, 2.3 A resolution
as apoprotein, 1.3 A resolution
crystallization of mutant delta R306, with Fe2+ and 2-oxoglutarate, 2.1 A resolution
crystallization of mutant delta R307A, with Fe2+, succinate and CO2, 1.96 A resolution
crystallization of wild-type enzyme and of the DELTAR306 mutant complexed with iron(II) and 2-oxoglutarate to 2.1 A and the DELTAR306A mutant complexed with iron(II), succinate and unhydrated carbon dioxide to 1.96 A
crystallization with 5-hydroxy-4-ketovaleric acid, 1.53 A resolution
crystallization with Fe(II) and succinate , 1.5 A resolution
crystallization with Fe(II) and deacetoxycephalosporin C, 1.7 A resolution
crystallization with Fe(II) and penicillin G, 1.6 A resolution
crystallization with Fe(II), 2-oxoglutarate and ampicillin, 1.5 A resolution
crystallization with Fe(II), 2-oxoglutarate and penicillin G, 1.7 A resolution
crystallization with Fe2+ and 2-oxoglutarate, 1.5 A resolution, the crystal structure of scDAOCS complexed with 2-oxoglutarate reveals that the 5-carboxylate of 2-oxoglutarate is stabilized by electrostatic interaction with the side chain of R258
crystallization with Fe2+, 1.5 A resolution
hanging drop method, recombinant enzyme expressed in Escherichia coli
quantum mechanical calculations of the first part of the reaction based on the high-resolution structures of the active site and its complexes with ligands
R258Q mutant, crystallization with Fe(II) and alpha-keto-beta-methylbutanoate, 1.5 and 1.6 A resolution
recombinant enzyme expressed in Escherichia coli, high-resolution structures for apoenzyme, the enzyme complexed with Fe(II), and with Fe(II) and 2-oxoglutarate
recombinant N-terminally His-tagged wild-type and C-terminally truncated mutant enzymes, free enzyme, or complexing with Fe2+, or Fe2+/ampicillin, hanging drop vapour diffusion method, 4°C, precipitant solution: 100 mM HEPES-NaOH, pH 8.0, 0.9-1.1 M ammonium sulfate, the reservoir solution is covered with oil to retard the evaporation, cryoprotection by 30% v/v ethylene glycol in precipitant solution, X-ray structure determination and analysis at 2.3 A resolution, molecular modeling
with N-terminal His tag and Fe2+, 2.51 A resolution
with N-terminal His tag, crystallization with ampicillin and Fe2+, 2.7 A resolution
with N-terminal His tag, crystallization with deacetoxycephalosporin C and Fe2+, 3.0 A resolution