1112-32-9

Basic information

• Product Name: (2S)-2,4-Dihydroxy-3,3-dimethylbutanoic acid
• Synonyms: (2S)-2,4-Dihydroxy-3,3-dimethylbutanoic acid;(S)-2,4-Dihydroxy-3,3-dimethylbutyric acid;[S,(-)]-2,4-Dihydroxy-3,3-dimethylbutyric acid;L-Pantoic acid;Dexpanthenol iMpurity C
• CAS NO: 1112-32-9
• Molecular Formula: C₆H₁₂O₄
• Molecular Weight: 148.16
• Mol File: 1112-32-9.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• CAS DataBase Reference: (2S)-2,4-Dihydroxy-3,3-dimethylbutanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (2S)-2,4-Dihydroxy-3,3-dimethylbutanoic acid(1112-32-9)
• EPA Substance Registry System: (2S)-2,4-Dihydroxy-3,3-dimethylbutanoic acid(1112-32-9)

Safety Data

• Hazardous Substances Data: 1112-32-9(Hazardous Substances Data)

Usage

General Description

(2S)-2,4-Dihydroxy-3,3-dimethylbutanoic acid, also known as alpha-ketoisocaproic acid or 2-KIC, is a chemical compound with the molecular formula C6H12O4. It is a keto acid derivative and a key intermediate in the metabolism of the essential amino acid leucine. 2-KIC has been found to have potential therapeutic applications for the treatment of various diseases and conditions, including diabetes, kidney disease, and muscle wasting. It is also being investigated for its potential role in enhancing athletic performance and recovery. Additionally, 2-KIC is a precursor to the production of the neurotransmitter GABA, which has implications for its potential use in the treatment of neurological disorders.

Upstream product

• 470-29-1 (+-)-2,4-dihydroxy-3,3-dimethyl-butyric acid 
• 79-50-5 (S)-pantolactone 
• 79-50-5 pantolactone 

Relevant articles and documents

Development of a Novel Biocatalyst for the Resolution of rac-Pantolactone

A novel L-pantolactone hydrolase, Lph, from Agrobacterium tumefaciens Lu681 was characterized, which stereospecifically hydrolyses L-pantolactone to L-pantoic acid yielding D-pantolactone with > 95% enantiomeric excess. The enzyme was found to be a 30 kDa-Zn2+-hydrolase with a Km for L-pantolactone of 7 mM and a Vmax of 30 U/mg. The corresponding lph gene was identified as an 807 bp ORF and cloned into E. coli. It was overexpressed under control of Ptac and Prha yielding enzyme activities of up to 600 U/g dry weight. Resolution of D,L-pantolactone in repeated batches with isolated Lph and enzyme recovery by membrane filtration gave D-pantolactone with 50% yield and 90-95% ee over 6 days. Covalent immobilization to EupergitC led to a stable biocatalyst easy to handle in a repeated batch production of D-pantolactone. Further improvements in the activity of Lph were achieved by directed evolution of the enzyme. Activities of mutants F62S, K197D and F100L were increased 2.3, 1.7, and 1.5 fold, respectively.