In enzymology, a deacetoxycephalosporin-C synthase (EC 1.14.20.1) is an enzyme that catalyzes the chemical reaction
| deacetoxycephalosporin-C synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.20.1 | ||||||||
| CAS no. | 85746-10-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The 3 substrates of this enzyme are penicillin N, 2-oxoglutarate, and O2, whereas its 4 products are deacetoxycephalosporin C, succinate, CO2, and H2O.
Classification
editThis 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 the other dehydrogenated.
Nomenclature
editThe systematic name of this enzyme class is penicillin-N,2-oxoglutarate:oxygen oxidoreductase (ring-expanding). Other names in common use include DAOCS, penicillin N expandase, and DAOC synthase.
Biological role
editThis enzyme participates in penicillin and cephalosporin biosynthesis.
Structural studies
editAs of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1UNB, 1UO9, 1UOB, 1UOF, 1UOG, 1W28, and 1W2A.
References
edit- Cantwell C, Beckmann R, Whiteman P, Queener SW, Abraham EP (1992). "Isolation of deacetoxycephalosporin C from fermentation broths of Penicillium chrysogenum transformants: construction of a new fungal biosynthetic pathway". Proceedings of the Royal Society B. 248 (1323): 283–9. Bibcode:1992RSPSB.248..283C. doi:10.1098/rspb.1992.0073. PMID 1354366. S2CID 40424189.
- Lee HJ, Lloyd MD, Harlos K, Clifton IJ, Baldwin JE, Schofield CJ (2001). "Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS)". J. Mol. Biol. 308 (5): 937–48. doi:10.1006/jmbi.2001.4649. PMID 11352583.
- Yeh WK, Ghag SK, Queener SW (1992). "Enzymes for epimerization of isopenicillin N, ring expansion of penicillin N, and 3'-hydroxylation of deacetoxycephalosporin C Function, evolution, refolding, and enzyme engineering". Ann. N.Y. Acad. Sci. 672: 396–408. doi:10.1111/j.1749-6632.1992.tb32705.x (inactive 2024-11-03).
{{cite journal}}: CS1 maint: DOI inactive as of November 2024 (link) - Andersson I; Van Scheltinga, AC; Lloyd, MD; Hara, T; Ramaswamy, S; Perrakis, A; Thompson, A; Lee, HJ; et al. (1998). "Structure of a cephalosporin synthase". Nature. 394 (6695): 805–9. Bibcode:1998Natur.394..805V. doi:10.1038/29575. PMID 9723623. S2CID 4361123.
- Dotzlaf JE, Yeh WK (1989). "Purification and properties of deacetoxycephalosporin C synthase from recombinant Escherichia coli and its comparison with the native enzyme purified from Streptomyces clavuligerus". J. Biol. Chem. 264 (17): 10219–27. doi:10.1016/S0021-9258(18)81788-4. PMID 2656705.
