ExplorEnz: EC 1.14.11.26

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1.14.11.26

Accepted name:

deacetoxycephalosporin-C hydroxylase

Reaction:

deacetoxycephalosporin C + 2-oxoglutarate + O₂ = deacetylcephalosporin C + succinate + CO₂

For diagram of cephalosporin biosynthesis, click here

Other name(s):

deacetylcephalosporin C synthase; 3′-methylcephem hydroxylase; DACS; DAOC hydroxylase; deacetoxycephalosporin C hydroxylase

Systematic name:

deacetoxycephalosporin-C,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)

Comments:

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.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 69772-89-0

References:

1.	Dotzlaf, J.E. and Yeh, W.K. Copurification and characterization of deacetoxycephalosporin C synthetase/hydroxylase from Cephalosporium acremonium. J. Bacteriol. 169 (1987) 1611–1618. [DOI] [PMID: 3558321]
2.	Baker, B.J., Dotzlaf, J.E. and Yeh, W.K. Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus. Purification, characterization, bifunctionality, and evolutionary implication. J. Biol. Chem. 266 (1991) 5087–5093. [PMID: 2002049]
3.	Coque, J.J., Enguita, F.J., Cardoza, R.E., Martin, J.F. and Liras, P. Characterization of the cefF gene of Nocardia lactamdurans encoding a 3′-methylcephem hydroxylase different from the 7-cephem hydroxylase. Appl. Microbiol. Biotechnol. 44 (1996) 605–609. [PMID: 8703431]
4.	Ghag, S.K., Brems, D.N., Hassell, T.C. and Yeh, W.K. Refolding and purification of Cephalosporium acremonium deacetoxycephalosporin C synthetase/hydroxylase from granules of recombinant Escherichia coli. Biotechnol. Appl. Biochem. 24 (1996) 109–119. [PMID: 8865604]
5.	Lloyd, M.D., Lipscomb, S.J., Hewitson, K.S., Hensgens, C.M., Baldwin, J.E. and Schofield, C.J. Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase. J. Biol. Chem. 279 (2004) 15420–15426. [DOI] [PMID: 14734549]
6.	Wu, X.B., Fan, K.Q., Wang, Q.H. and Yang, K.Q. C-terminus mutations of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase with improved activity toward penicillin analogs. FEMS Microbiol. Lett. 246 (2005) 103–110. [DOI] [PMID: 15869968]
7.	Martín, J.F., Gutiérrez, S., Fernández, F.J., Velasco, J., Fierro, F., Marcos, A.T. and Kosalkova, K. Expression of genes and processing of enzymes for the biosynthesis of penicillins and cephalosporins. Antonie Van Leeuwenhoek 65 (1994) 227–243. [PMID: 7847890]

[EC 1.14.11.26 created 2005]