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Usage

Uses

Used in Pharmaceutical Industry:
(R)-5-CHLORO-2-PENTANOL is used as an intermediate in the synthesis of pharmaceuticals for its ability to contribute to the development of new medications.
Used in Agrochemical Industry:
(R)-5-CHLORO-2-PENTANOL is used as an intermediate in the production of agrochemicals, playing a role in the creation of substances that help protect and enhance crop yields.
Used in Fragrance Industry:
(R)-5-CHLORO-2-PENTANOL is used as an intermediate in the synthesis of fragrances, contributing to the development of new scents for various applications.
Used as a Chiral Building Block:
(R)-5-CHLORO-2-PENTANOL is used as a chiral building block in the synthesis of chiral pharmaceuticals and other fine chemicals, highlighting its importance in the production of enantiomerically pure compounds.
It is crucial to handle (R)-5-CHLORO-2-PENTANOL with care due to its potential harmful effects if ingested, inhaled, or absorbed through the skin.

InChI:InChI=1/C5H11ClO/c1-5(7)3-2-4-6/h5,7H,2-4H2,1H3/t5-/m0/s1

Upstream product

• 5891-21-4 5-chloro-2-pentanone 

Relevant academic research and scientific papers

Practical application of recombinant whole-cell biocatalysts for the manufacturing of pharmaceutical intermediates such as chiral alcohols

We have developed efficient biocatalytic processes for the preparation of chiral alcohols, such as (R)-1,3-butanediol, ethyl (S)-4-chloro-3-hyroxybutanoate, ethyl (R)-4-chloro-3-hyroxybutanoate, (S)-5-chloro-2-pentanol, (R)-5-chloro-2-pentanol, and (S)-cyclopropylethanol by stereospecific enzymatic oxidoreduction on a practical level. These chiral alcohols are very important synthons for the synthesis of various pharmaceutical intermediates that lead to antibiotics and inhibitors of HMG-CoA reductase. Here, we present practical applications on biocatalysis using novel recombinant whole-cell biocatalysts that catalyzed enantioselective oxidation and asymmetric reduction with a coenzyme regeneration system.

A Pseudomonas sp. Alcohol Dehydrogenase with Broad Substrate Specificity and Unusual Stereospecificity for Organic Synthesis

A new alcohol dehydrogenase from Pseudomonas sp. strian PED has been isolated and characterized.The enzyme exhibits a broad substrate specificity, accepting aromatic, cyclic, and aliphatic compounds as substrates.The Km values were determined as 525 μM for NAD and 75 μM for 2-propanol with a specific activity of 36 U/mg.The kinetic mechanism is ordered bi-bi with the cofactor binding first and releasing last.The enzyme transfers the pro-R hydride of NADH to the si face of carbonyl compounds to yield (R) alcohols.Synthetic-scale reductions of a number of representative compounds were carried out in high enentiomeric excess with in situ regeneration of NADH using 2-propanol as the hydride source and the same enzyme as catalyst.

Lactobacillus kefir Alcohol Dehydrogenase: A Useful Catalyst for Synthesis

The alcohol dehydrogenase from Lactobacillus kefir simultaneously catalyzes carbonyl reductions and NADPH regeneration in the presence of 2-propanol.Representative synthesis of a number of chiral alcohols was accomplished in good yield and high enantiomeric excess (94-99percent).This NADPH-requiring enzyme transfers the pro-R hydride from the cofactor to the si face of carbonyls to give (R) alcohols.The enzyme exhibits a very broad substrate specificity and high enantioselectivity for the synthesis of chiral aromatic, cyclic, polycyclic, and aliphatic alcohols.

A New NAD-dependent Alcohol Dehydrogenase with Opposite Facial Selectivity useful for Asymmetric Reduction and Cofactor Regeneration

A new NAD-dependent alcohol dehydrogenase isolated from a Pseudomonas species catalysed the reduction of many acyclic ketones to optically active alcohols with very high enantioselectivity (90 to >98percent enantiomeric excess); the stereochemical course of the reduction was determined to be the transfer of the pro-(R) hydrogen from NADH to the Si face of the carbonyl group, a process different from that for other known alcohol dehydrogenases.