116233-49-9

Upstream product

• 70681-41-3 (R)-dimethyl malate 
• 81927-55-1 O-benzyl 2,2,2-trichloroacetimidate 
• 134356-95-9 dimethyl 2-(benzyloxy)succinate 
• 100-39-0 benzyl bromide 
• 38115-87-6 malic acid dimethyl ester 

Downstream Products

• 82130-73-2 dimethyl (S)-(-)-2-benzyloxybutanedioate 
• 86185-81-1 2-(benzyloxy)-1,4-butanediol 
• 342892-28-8 benzoxysuccinic acid 
• 68363-71-3 3-benzyloxytetrahydrofuran 
• 123394-80-9 (2S)-2-phenylmethoxybutane-1,4-diol 
• 134298-54-7 (R)-2-Benzyloxy-succinic acid 4-methyl ester 
• 1346538-64-4 C₂₃H₂₅O₆P 
• 1346538-67-7 C₃₅H₃₄O₉P₂ 
• 1346538-70-2 (R)-3-(benzyloxy)-4-oxobutyl diphenyl phosphate 
• 1346538-71-3 (R)-3-(benzyloxy)-4,4-dimethoxybutyl diphenyl phosphate 
• 134298-54-7 (S)-2-Benzyloxy-succinic acid 4-methyl ester 

Relevant academic research and scientific papers

Synthesis of 3-substituted tetrahydrofuran and 4-substituted tetrahydropyran derivatives by cyclization of dicarboxylic acids with InBr 3/TMDS

An efficient reduction followed by cyclization of diacid compounds with the InBr3/TMDS system is reported. This system allows the formation of five- and six-membered ring ethers substituted in the 3- or 4-position. Copyright

Investigating the role of the hydroxyl groups of substrate erythrose 4-phosphate in the reaction catalysed by the first enzyme of the shikimate pathway

3-Deoxy-d-arabino-heptulosonate 7-phosphate (DAH7P) synthase catalyses the first step of the shikimate pathway, which is responsible for the biosynthesis of aromatic amino acids in microorganisms and plants. This enzyme catalyses an aldol reaction between phosphoenolpyruvate and d-erythrose 4-phosphate to generate DAH7P. Both 2-deoxyerythrose 4-phosphate and 3-deoxyerythrose 4-phosphate were synthesised and tested as alternative substrates for the enzyme. Both compounds were found to be substrates for the DAH7P synthases from Escherichia coli, Pyrococcus furiosus and Mycobacterium tuberculosis, consistent with an acyclic mechanism for the enzyme for which neither C2 nor C3 hydroxyl groups are required for catalysis. The enzymes all showed greater tolerance for the loss of the C2 hydroxyl group than the C3 hydroxyl group.

A Biocatalytic Approach to the Enantioselective Synthesis of (R)- and (S)-Malic Acid

(S)-Diethyl malate 1a was prepared (70-80percent yield; >98percent optical purity) by an enantioselective reduction of sodium diethyl oxalacetate 2 by fermenting baker's yeast (Saccharomyces cerevisiae).Other microorganisms were tested for their capability of reducing 2.Most of them afforded (S)-1a with ee from 8 to 94percent and only Candida utilis, Aspergillus niger and Lactobacillus fermentum ILC G18D preferentially reduced compound 2 to (R)-1a. (R)-Dimethyl malate 1b was obtained from (R,S)-malate 1b by hydrolysis with pig liver esterase (PLE), the highest ee (93percent) being realized at 0 deg C in 20percent aqueous methanol.Enzymatic hydrolyses of protected malates 1d and 1e did not lead to improvement of the ee.