Deacetoxycephalosporin-C synthase

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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a deacetoxycephalosporin-C synthase (EC 1.14.20.1) is an enzyme that catalyzes the chemical reaction

penicillin N + 2-oxoglutarate + O₂${\displaystyle \rightleftharpoons }$ deacetoxycephalosporin C + succinate + CO₂ + H₂O

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

• 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 30 July 2025).
• 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.