In enzymology, a deacetoxycephalosporin-C hydroxylase (EC 1.14.11.26) is an enzyme that catalyzes the chemical reaction
| Deacetoxycephalosporin-C hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.26 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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- deacetoxycephalosporin C + 2-oxoglutarate + O2 deacetylcephalosporin C + succinate + CO2
The 3 substrates of this enzyme are deacetoxycephalosporin C, 2-oxoglutarate, and O2, whereas its 3 products are deacetylcephalosporin C, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is deacetoxycephalosporin-C,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include deacetylcephalosporin C synthase, 3'-methylcephem hydroxylase, DACS, DAOC hydroxylase, and deacetoxycephalosporin C hydroxylase. This enzyme participates in penicillin and cephalosporin biosynthesis.
References edit
- Dotzlaf JE, Yeh WK (1987). "Copurification and characterization of deacetoxycephalosporin C synthetase/hydroxylase from Cephalosporium acremonium". J. Bacteriol. 169 (4): 1611–8. PMC 211989. PMID 3558321.
- Baker BJ, Dotzlaf JE, Yeh WK (1991). "Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus Purification, characterization, bifunctionality, and evolutionary implication". J. Biol. Chem. 266 (8): 5087–93. PMID 2002049.
- Coque JJ, Enguita FJ, Cardoza RE, Martin JF, Liras P (1996). "Characterization of the cefF gene of Nocardia lactamdurans encoding a 3'-methylcephem hydroxylase different from the 7-cephem hydroxylase". Appl. Microbiol. Biotechnol. 44 (5): 605–9. doi:10.1007/BF00172492. PMID 8703431.
- Ghag SK, Brems DN, Hassell TC, Yeh WK. "Refolding and purification of Cephalosporium acremonium deacetoxycephalosporin C synthetase/hydroxylase from granules of recombinant Escherichia coli". Biotechnol. Appl. Biochem. 24: 109–19. PMID 8865604.
- Schofield CJ; Lipscomb, SJ; Hewitson, KS; Hensgens, CM; Baldwin, JE; Schofield, CJ (2004). "Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase". J. Biol. Chem. 279 (15): 15420–6. doi:10.1074/jbc.M313928200. PMID 14734549.
- Wu XB, Fan KQ, Wang QH, Yang KQ (2005). "C-terminus mutations of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase with improved activity toward penicillin analogs". FEMS Microbiol. Lett. 246 (1): 103–10. doi:10.1016/j.femsle.2005.03.043. PMID 15869968.
- AT, Kosalkova K; Gutiérrez, S; Fernández, FJ; Velasco, J; Fierro, F; Marcos, AT; Kosalkova, K (1994). "Expression of genes and processing of enzymes for the biosynthesis of penicillins and cephalosporins". Antonie van Leeuwenhoek. 65 (3): 227–43. doi:10.1007/BF00871951. PMID 7847890.
