- Classification
- Nomenclature
- Biological role
- Structural studies
- References
| Name = deacetoxycephalosporin-C synthase
| EC_number = 1.14.20.1
| CAS_number = 85746-10-7
| IUBMB_EC_number = 1/14/20/1
| GO_code = 0050599
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In enzymology, a deacetoxycephalosporin-C synthase ({{EC number|1.14.20.1}}) is an enzyme that catalyzes the chemical reaction
deacetoxycephalosporin C + succinate + CO2 + H2OThe 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 {{PDB link|1UNB}}, {{PDB link|1UO9}}, {{PDB link|1UOB}}, {{PDB link|1UOF}}, {{PDB link|1UOG}}, {{PDB link|1W28}}, and {{PDB link|1W2A}}.
References
- {{cite journal | vauthors = Cantwell C, Beckmann R, Whiteman P, Queener SW, Abraham EP | date = 1992 | title = Isolation of deacetoxycephalosporin C from fermentation broths of Penicillium chrysogenum transformants: construction of a new fungal biosynthetic pathway | journal = Proceedings of the Royal Society B | volume = 248 | pages = 283–9 | pmid = 1354366 | doi = 10.1098/rspb.1992.0073 | issue = 1323 }}
- {{cite journal | vauthors = Lee HJ, Lloyd MD, Harlos K, Clifton IJ, Baldwin JE, Schofield CJ | date = 2001 | title = Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS) | journal = J. Mol. Biol. | volume = 308 | pages = 937–48 | pmid = 11352583 | doi = 10.1006/jmbi.2001.4649 | issue = 5 }}
- {{cite journal | vauthors = Yeh WK, Ghag SK, Queener SW | last-author-amp = yes | date = 1992 | title = Enzymes for epimerization of isopenicillin N, ring expansion of penicillin N, and 3'-hydroxylation of deacetoxycephalosporin C Function, evolution, refolding, and enzyme engineering | journal = Ann. N.Y. Acad. Sci. | volume = 672 | pages = 396–408 | doi = 10.1111/j.1749-6632.1992.tb32705.x }}
- {{cite journal | author = Andersson I | date = 1998 | title = Structure of a cephalosporin synthase | journal = Nature | volume = 394 | pages = 805–9 | pmid = 9723623 | doi = 10.1038/29575 | last2 = Van Scheltinga | first2 = AC | last3 = Lloyd | first3 = MD | last4 = Hara | first4 = T | last5 = Ramaswamy | first5 = S | last6 = Perrakis | first6 = A | last7 = Thompson | first7 = A | last8 = Lee | first8 = HJ | last9 = Baldwin | first9 = JE | last10 = Lee | first10 = Hwei-Jen | last11 = Baldwin | first11 = Jack E. | last12 = Hajdu | first12 = Janos | issue = 6695 | display-authors = 8 }}
- {{cite journal | vauthors = Dotzlaf JE, Yeh WK | date = 1989 | title = Purification and properties of deacetoxycephalosporin C synthase from recombinant Escherichia coli and its comparison with the native enzyme purified from Streptomyces clavuligerus | journal = J. Biol. Chem. | volume = 264 | pages = 10219–27 | pmid = 2656705 | issue = 17 }}