期刊
BIOCHEMISTRY
卷 53, 期 15, 页码 2483-2493出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi500086p
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资金
- Wellcome Trust
- European Research Council
- Biotechnology & Biological Sciences Research Council (BBSRC)
- Clarendon - St Hugh's College - W. Louey Scholarship
- Open Horizons program of the Dinu Patriciu Foundation
- British Heart Foundation
- Berrow Foundation
- Royal Society Dorothy Hodgkin Fellowship
- L'Oreal-UNESCO For Women in Science Fellowship
- BBSRC [BB/J003018/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/J003018/1] Funding Source: researchfish
Deacetoxycephalosporin C synthase (DAOCS) catalyzes the oxidative ring expansion of penicillin N (penN) to give deacetoxycephalosporin C (DAOC), which is the committed step in the biosynthesis of the clinically important cephalosporin antibiotics. DAOCS belongs to the family of non-heme iron(II) and 2-oxoglutarate (2OG) dependent oxygenases, which have substantially conserved active sites and are proposed to employ a consensus mechanism proceeding via formation of an enzyme.Fe(II).2OG.substrate ternary complex. Previously reported kinetic and crystallographic studies led to the proposal of an unusual ping-pong mechanism for DAOCS, which was significantly different from other members of the 2OG oxygenase superfamily. Here we report pre-steady-state kinetics and binding studies employing mass spectrometry and NMR on the DAOCS-catalyzed penN ring expansion that demonstrate the viability of ternary complex formation in DAOCS catalysis, arguing for the generality of the proposed consensus mechanism for 2OG oxygenases.
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