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
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1.14.20.1
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clavuligerus
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chrysogenum
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acremonium
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isopenicillin
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penicillium
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beta-lactams
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epimerase
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cephamycins
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cephalosporium
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ring-expansion
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7-aminodeacetoxycephalosporanic
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pcbab
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ironii
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cephem
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lactamdurans
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synthesis
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7-adca
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2-oxoglutarate-dependent
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cephalexin
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carbenicillin
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doacs
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biotechnology
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medicine
- 1.14.20.1
- clavuligerus
- chrysogenum
- acremonium
- isopenicillin
- penicillium
- beta-lactams
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epimerase
-
cephamycins
- cephalosporium
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ring-expansion
-
7-aminodeacetoxycephalosporanic
-
pcbab
-
ironii
-
cephem
- lactamdurans
- synthesis
-
7-adca
-
2-oxoglutarate-dependent
- cephalexin
- carbenicillin
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doacs
- biotechnology
- medicine
Reaction
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
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General Information
General Information on EC 1.14.20.1 - deacetoxycephalosporin-C synthase
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evolution
metabolism
physiological function
additional information
DAOCS is classified to the 2-oxoglutarate-Fe(II)-dioxygenase superfamily
evolution
the enzyme belongs to the iron- and 2-oxoglutarate-dependent oxidases
evolution
the enzyme belongs to the iron- and 2-oxoglutarate-dependent oxidases
evolution
the enzyme belongs to the iron- and 2-oxoglutarate-dependent oxidases
evolution
the enzyme is a member of the 2-oxoglutarate oxygenase superfamily, the members have substantially conserved active sites and are proposed to employ a consensus mechanism proceeding via formation of an enzyme·Fe(II)-2OG-substrate ternary complex
evolution
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the enzyme is a member of the 2-oxoglutarate oxygenase superfamily, the members have substantially conserved active sites and are proposed to employ a consensus mechanism proceeding via formation of an enzyme·Fe(II)-2OG-substrate ternary complex
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evolution
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the enzyme belongs to the iron- and 2-oxoglutarate-dependent oxidases
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the enzyme from Acremonium chrysogenum is bifunctional and catalyzes both the synthesis of deacetoxycephalosporin C from penicillin N, EC 1.14.20.1, as well as the hydroxylation of deacetoxycephalosporin C to deacetylcephalosporin C, EC 1.14.11.26. The activities are located on two different domains
metabolism
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the enzyme from Acremonium chrysogenum is bifunctional and catalyzes both the synthesis of deacetoxycephalosporin C from penicillin N, EC 1.14.20.1, as well as the hydroxylation of deacetoxycephalosporin C to deacetylcephalosporin C, EC 1.14.11.26. The activities are located on two different domains
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Cephalosporium acremonium expandase is a bifunctional enzyme, penicillin expandase, which catalyzes the ring expansion of penicillin N and the hydroxylation of deacetoxycephalosporin C (DAOC) to deacetylcephalosporin C (DAC). 2-oxoglutarate, Fe2+ and O2 are required for its catalytic activity. The enzyme is encoded by gene cefEF
physiological function
Cephalosporium acremonium expandase is a bifunctional enzyme, which catalyzes the ring expansion of penicillin N and the hydroxylation of deacetoxycephalosporin C (DAOC) to deacetylcephalosporin C (DAC). 2-oxoglutarate, Fe2+ and O2 are required for its catalytic activity. The enzyme is encoded by gene cefEF
physiological function
deacetoxycephalosporin C synthase (DAOCS) catalyzes the oxidative ring expansion of penicillin N (penN) to give deacetoxycephalosporin C (DAOC), which is the committed step in the biosynthesis of the clinically important cephalosporin antibiotics. The enzyme from Streptomyces clavuligerus shows an unusual ping-pong mechanism, which is significantly different from other members of the 2OG oxygenase superfamily
physiological function
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deacetoxycephalosporin C synthase (DAOCS) catalyzes the oxidative ring expansion of penicillin N (penN) to give deacetoxycephalosporin C (DAOC), which is the committed step in the biosynthesis of the clinically important cephalosporin antibiotics. The enzyme from Streptomyces clavuligerus shows an unusual ping-pong mechanism, which is significantly different from other members of the 2OG oxygenase superfamily
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additional recombinant expression of gene cefF from Streptomyces clavuligerus in Acremonium chrysogenum strain CGMCC3.3795 leads to a reduction of the content of deacetoxycephalosporin C in the cephalosporin C fermentation broth, quantitative PCR expression analysis, overview
additional information
structure simulations, docking, and modeling, active site prediction, residues R162, F164, M180, L204, V245, V262, F264, and I305 are involved in 2-oxoglutarate binding, overview
additional information
determination of formation of a DAOCS·Fe(II)-2OG-penicillin N complex by nondenaturing ESI-MS analyses
additional information
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additional recombinant expression of gene cefF from Streptomyces clavuligerus in Acremonium chrysogenum strain CGMCC3.3795 leads to a reduction of the content of deacetoxycephalosporin C in the cephalosporin C fermentation broth, quantitative PCR expression analysis, overview
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additional information
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determination of formation of a DAOCS·Fe(II)-2OG-penicillin N complex by nondenaturing ESI-MS analyses
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