KEGG   ENZYME: 1.14.11.26Help
Entry
EC 1.14.11.26               Enzyme                                 

Name
deacetoxycephalosporin-C hydroxylase;
deacetylcephalosporin C synthase;
3'-methylcephem hydroxylase;
DACS;
DAOC hydroxylase;
deacetoxycephalosporin C hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
BRITE hierarchy
Sysname
deacetoxycephalosporin-C,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Reaction(IUBMB)
deacetoxycephalosporin C + 2-oxoglutarate + O2 = deacetylcephalosporin C + succinate + CO2 [RN:R05229]
Reaction(KEGG)
Substrate
deacetoxycephalosporin C [CPD:C06565];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
deacetylcephalosporin C [CPD:C03112];
succinate [CPD:C00042];
CO2 [CPD:C00011]
Comment
Requires iron(II). The enzyme can also use 3-exomethylenecephalosporin C as a substrate to form deacetoxycephalosporin C, although more slowly [2]. In Acremonium chrysogenum, the enzyme forms part of a bifunctional protein along with EC 1.14.20.1, deactoxycephalosporin-C synthase. It is a separate enzyme in Streptomyces clavuligerus.
History
EC 1.14.11.26 created 2005
Pathway
Penicillin and cephalosporin biosynthesis
Metabolic pathways
Biosynthesis of antibiotics
Orthology
K12745  
deacetoxycephalosporin-C hydroxylase
Genes
SCT: 
SCAT_5681(cefF)
SCY: 
Taxonomy
Reference
1  [PMID:3558321]
  Authors
Dotzlaf JE, Yeh WK.
  Title
Copurification and characterization of deacetoxycephalosporin C synthetase/hydroxylase from Cephalosporium acremonium.
  Journal
J. Bacteriol. 169 (1987) 1611-8.
Reference
2  [PMID:2002049]
  Authors
Baker BJ, Dotzlaf JE, Yeh WK.
  Title
Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus. Purification, characterization, bifunctionality, and evolutionary implication.
  Journal
J. Biol. Chem. 266 (1991) 5087-93.
  Sequence
Reference
3  [PMID:8703431]
  Authors
Coque JJ, Enguita FJ, Cardoza RE, Martin JF, Liras P.
  Title
Characterization of the cefF gene of Nocardia lactamdurans encoding a 3'-methylcephem hydroxylase different from the 7-cephem hydroxylase.
  Journal
Appl. Microbiol. Biotechnol. 44 (1996) 605-9.
  Sequence
Reference
4  [PMID:8865604]
  Authors
Ghag SK, Brems DN, Hassell TC, Yeh WK.
  Title
Refolding and purification of Cephalosporium acremonium deacetoxycephalosporin C synthetase/hydroxylase from granules of recombinant Escherichia coli.
  Journal
Biotechnol. Appl. Biochem. 24 ( Pt 2) (1996) 109-19.
Reference
5  [PMID:14734549]
  Authors
Lloyd MD, Lipscomb SJ, Hewitson KS, Hensgens CM, Baldwin JE, Schofield CJ.
  Title
Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase.
  Journal
J. Biol. Chem. 279 (2004) 15420-6.
Reference
6  [PMID:15869968]
  Authors
Wu XB, Fan KQ, Wang QH, Yang KQ.
  Title
C-terminus mutations of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase with improved activity toward penicillin analogs.
  Journal
FEMS. Microbiol. Lett. 246 (2005) 103-10.
Reference
7  [PMID:7847890]
  Authors
Martin JF, Gutierrez S, Fernandez FJ, Velasco J, Fierro F, Marcos AT, Kosalkova K.
  Title
Expression of genes and processing of enzymes for the biosynthesis of penicillins and cephalosporins.
  Journal
Antonie. Van. Leeuwenhoek. 65 (1994) 227-43.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
69772-89-0

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