92685-81-9

Upstream product

• 20781-20-8 2,4-Dimethoxybenzylamine 
• 5437-45-6 Benzyl bromoacetate 
• 1738-68-7 Gly-OBz 
• 613-45-6 2,4-Dimethoxybenzaldehyde 

Downstream Products

• 912296-79-8 N-benzoyl-N-(2,4-dimethoxybenzyl)glycine benzyl ester 
• 92685-88-6 (2S,3S)-1-(2,4-Dimethoxy-benzyl)-3-((R)-1-hydroxy-ethyl)-4-oxo-azetidine-2-carboxylic acid benzyl ester 
• 912296-80-1 2-[benzoyl(2,4-dimethoxybenzyl)amino]malonic acid benzyl ester 3-(benzyloxycarbonyl)phenyl ester 
• 912296-81-2 2-(benzoylamino)malonic acid benzyl ester 3-(benzyloxycarbonyl)phenyl ester 

Relevant academic research and scientific papers

STEREOSPECIFIC SYNTHESIS OF CHIRAL PRECURSORS OF THIENAMYCIN FROM L-THREONINE

L-Threonine was transformed, stereospecifically, to a versatile β-lactam (5a) in 3 steps.This β-lactam was further converted to a key intermediate (25) for the synthesis of thienamycin and its biologically active analogues.Furthermore, the compound 5a was changed to iodides (18 and 23), cyanides (19 and 24), chloromethylketone (26) and aldehydes (30 and 31) which appear to have a latent potential as precursors for the syntheses of the carbapenems.

Synthesis and β-lactamase reactivity of α-substituted phenaceturates

β-Lactams with 6α (penicillins) or 7α (cephalosporins) substituents are often β-lactamase inhibitors. This paper assesses the effect of such substituents on acyclic β-lactamase substrates. Thus, a series of m-carboxyphenyl phenaceturates, substituted at the glycyl α-carbon by -OMe, -CH2OH, -CO2-, and -CH2NH3+, have been prepared, and tested for their reactivity against serine β-lactamases. The latter two are novel substituents in β-lactamase substrates. The methoxy and hydroxymethyl compounds were found to be poor to moderately good substrates, depending on the enzyme. The aminomethyl compound gave rise to a transiently stable (t1/2 = 4.6 s) complex on its reaction with a class C β-lactamase. The reactivity of the compounds against three low molecular weight dd-peptidases was also tested. Again, the methoxy and hydroxymethyl compounds proved to be quite good substrates with no sign of inhibitory complexes. The dd-peptidases reacted with one enantiomer (the compounds were prepared as racemates), presumably the d compound. The class C β-lactamase reacted with both d and l enantiomers although it preferred the latter. The structural bases of these stereo-preferences were explored by reference to the crystal structure of the enzyme by molecular modeling studies. The aminomethyl compound was unreactive with the dd-peptidases, whereas the carboxy compound did not react with any of the above-mentioned enzymes. The inhibitory effects of the -OMe and -CH2OH substituents in β-lactams apparently require a combination of the substituent and the pendant leaving group of the β-lactam at the acyl-enzyme stage.