Biology:Deacetoxycephalosporin-C synthase
| deacetoxycephalosporin-C synthase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.14.20.1 | ||||||||
| CAS number | 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 | ||||||||
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In enzymology, a deacetoxycephalosporin-C synthase (EC 1.14.20.1) is an enzyme that catalyzes the chemical reaction
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
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 the other dehydrogenated.
Nomenclature
The 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
This enzyme participates in penicillin and cephalosporin biosynthesis.
Structural studies
As 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
- "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. 1992. doi:10.1098/rspb.1992.0073. PMID 1354366. Bibcode: 1992RSPSB.248..283C.
- "Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS)". J. Mol. Biol. 308 (5): 937–48. 2001. doi:10.1006/jmbi.2001.4649. PMID 11352583.
- "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. 1992. doi:10.1111/j.1749-6632.1992.tb32705.x.
- 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. doi:10.1038/29575. PMID 9723623. Bibcode: 1998Natur.394..805V.
- "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. 1989. PMID 2656705.
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