388568-32-9

Upstream product

• 100-39-0 benzyl bromide 
• 551-16-6 6-Aminopenicillanic Acid 
• 36273-76-4 6β-(4-nitro-benzylideneamino)-penicillanic acid benzyl ester 
• 3956-31-8 benzyl (2S,5R,6R)-6-amino-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylate 
• 36273-77-5 (5R)-3,3,6c-trimethyl-6t-(4-nitro-benzylideneamino)-7-oxo-(5rH)-4-thia-1-aza-bicyclo[3.2.0]heptane-2c-carboxylic acid benzyl ester 
• 36273-78-6 (5R)-6t-amino-3,3,6c-trimethyl-7-oxo-(5rH)-4-thia-1-aza-bicyclo[3.2.0]heptane-2c-carboxylic acid benzyl ester 
• 74271-82-2 N-(p-nitrobenzyloxycarbonyl)-D-α-aminoadipic acid 1-p-nitrobenzyl ester 

Relevant academic research and scientific papers

Contrasting fates for 6-α-methylpenicillin N upon oxidation by deacetoxycephalosporin C synthase (DAOCS) and deacetoxy/deacetylcephalosporin C synthase (DAOC/DACS)

6-α-Methylpenicillin N was synthesised via known routes from 6-aminopenicillanic acid, and tested as a substrate for recombinant DAOCS and DAOC/DACS. Incubation with DAOCS resulted in conversion of 2-oxoglutarate without oxidation of the penicillin substrate ('uncoupled turnover'). Incubation with DAOC/DACS resulted in oxidation to the cephem aldehyde. This is the first example of substrate-induced 'uncoupled turnover', which has been proposed to be an editing mechanism for these enzymes. Elsevier Science Ltd. All rights reserved.