5094-24-6

Usage

InChI:InChI=1/C4H8O3/c1-2-3(5)4(6)7/h3,5H,2H2,1H3,(H,6,7)/p-1/t3-/m1/s1

Upstream product

• 2013-26-5 2-oxobutyric acid, sodium salt 
• 3347-90-8 (2S)-2-hydroxybutanoic acid 

Downstream Products

• 110298-82-3 2-Benzyloxy-butyric acid benzyl ester 
• 130516-25-5 Benzyl 2-hydroxybutanoate 
• 600-15-7 2-Hydroxybutanoic acid 
• 41358-69-4 triethyl 2-oxa-1,3,3-butanetricarboxylate 
• 132513-51-0 n-butyl (S)-2-hydroxybutanoate 

Relevant academic research and scientific papers

Method for Improving Optical Purity of 2-Hydroxycarboxylic Acid or Derivative Thereof

To provide a method for improving optical purity of an optically active 2-hydroxycarboxylic acid or a derivative thereof, which is useful as a raw material in the manufacture of medicines, agrochemicais, and industrial products. The method of the invention for improving purity of a hydroxycarboxylic acid of the following formula (1a) or (1b) or a derivative thereof includes the steps of reacting the hydroxycarboxylic acid of the following formula (1a) or (1b) with at least one optically inactive base selected from the group consisting of an alkali metal, alkoxide and a secondary amine in the presence of a solvent and, subsequently, performing recrystallization, to thereby form a hydroxycarboxylic acid salt of the following formula (IIIa) or (IIIb): wherein R1 represents a C1-8 alkyl group, and R2 represents an alkali metal or a secondary amine.

A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases

The gene for the D-mandelate dehydrogenase (DManDH) of Enterococcus faecalis IAM10071 was isolated by means of an activity staining procedure and PCR and expressed in Escherichia coli cells. The recombinant enzyme exhibited high catalytic activity toward various 2-ketoacid substrates with bulky hydrophobic side chains, particularly C3-branched substrates such as benzoylformate and 2-ketoisovalerate, and strict coenzyme specificity for NADH and NAD+. It showed marked sequence similarity with known NADP-dependent 2-ketopantoate reductases (KPR). These results indicate that together with KPR, D-ManDH constitutes a new family of D-2-hydroxyacid dehydrogenases that act on C3-branched 2-ketoacid substrates with various specificities for coenzymes and substrates.