26924-74-3

Basic information

• Product Name: deacetoxycephalosporin C
• Synonyms: deacetoxycephalosporin C;(6R)-3-Methyl-7α-[[(R)-5-amino-5-carboxy-1-oxopentyl]amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]octa-2-ene-2-carboxylic acid;(6R,7R)-7-[[(R)-5-Amino-5-carboxy-1-oxopentyl]amino]-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid;Antibiotic WS-3442A;WS-3442A
• CAS NO: 26924-74-3
• Molecular Formula: C₁₄H₁₉N₃O₆S
• Molecular Weight: 357.38216
• Mol File: 26924-74-3.mol

Chemical Properties

• Boiling Point: 786.3°Cat760mmHg
• Flash Point: 429.3°C
• Appearance: /
• Density: 1.54g/cm³
• Vapor Pressure: 4.1E-27mmHg at 25°C
• Refractive Index: 1.654
• CAS DataBase Reference: deacetoxycephalosporin C(CAS DataBase Reference)
• NIST Chemistry Reference: deacetoxycephalosporin C(26924-74-3)
• EPA Substance Registry System: deacetoxycephalosporin C(26924-74-3)

Safety Data

• Hazardous Substances Data: 26924-74-3(Hazardous Substances Data)

Usage

InChI:InChI=1/C14H19N3O6S/c1-6-5-24-12-9(11(19)17(12)10(6)14(22)23)16-8(18)4-2-3-7(15)13(20)21/h7,9,12H,2-5,15H2,1H3,(H,16,18)(H,20,21)(H,22,23)/t7-,9-,12-/m1/s1

Upstream product

• 525-94-0 penicillin N 
• 328-50-7 α-ketoglutaric acid 

Relevant articles and documents

Studies on deacetoxycephalosporin C synthase support a consensus mechanism for 2-oxoglutarate dependent oxygenases

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.

Cephalosporin biosynthesis: A branched pathway sensitive to an isotope effect

Incubation of penicillin N (3a) with partially purified deacetoxy/deacetylcephalosporin C synthase (DAOC/DAC synthase) from Cephalosporium acremonium CO 728 gave in addition to the expected products, deacetoxycephalosporin C and deacetylcephalosporin C, a third β-lactam metabolite as a 3β-hydroxy-3α-methylcepham (9a). Production of the 3β-hydroxycepham was promoted from [3-2H]penicillin N (3b) which was rationalised by the operation of a kinetic isotope effect on a branched pathway in the enzymic process. The oxygen of the 3β-hydroxy group was shown to be derived in part from molecular oxygen. In addition, the 2β-methyl group of penicillin N was shown to be incorporated into C2 of the 3β-hydroxy-3α-methylcepham, a result in stereochemical accord with the equivalent transformation of the 2β-methyl group of penicillin N into C2 of deacetoxycephalosporin C1. A mechanistic interpretation, consistent with these observations, is offered.

Cephalosporin C Biosynthesis; a Branched Pathway Sensitive to a Kinetic Isotope Effect

Incubation of penicillin N with preparations of deacetoxycephalosporin C/deacetylcephalosporin C synthetase activity from Cephalosporium acremonium CO 728 gave, along with the normal product deacetoxycephalosporin C, another β-lactam metabolite, namely 7β--3β-hydroxy-3α-methyl4-2H)-cepham-4α-carboxylic acid.This material arises as a result of a deuterium isotope effect on a branched pathway in the enzymic mechanism.The 3β-hydroxy group in this substance arises from molecular oxygen.

Enzymatic Ring Expansion of Penicillins to Cephalosporins: Side Chain Specificity

Structural variants on the acylamino-side chains of penicillins as substrates for the ring expansion enzyme from Cephalosporium acremonium CO728 show that a six carbon chain terminating in a carboxy group permits efficient conversion into cephems with the expection of δ-(L-aminoadipoyl) .

THE ENZYMATIC RING EXPANSION OF PENICILLINS TO CEPHALOSPORINS: SIDE CHAIN SPECIFICITY

Structural variants of the acylamino side chain of penicillins have been tested as substrates for Deacetoxy/Deacetyl Cephalosporin C Synthetase from C. acremonium CO 728.A six carbon chain terminating in a carboxyl group was found to permit efficient ring expansion to cephems, with the exception of δ-(L-α-aminoadipoyl).