99212-19-8

Upstream product

• 5891-21-4 5-chloro-2-pentanone 

Downstream Products

• 102108-40-7 phenyl (2R,6S)-(trans-6-methyltetrahydropyran-2-yl)acetate 
• 102208-94-6 (2R,6S)-(trans-6-methyltetrahydropyran-2-yl)acetophenone 
• 102208-95-7 (2S,6S)-(cis-6-methyltetrahydropyran-2-yl)acetophenone 
• 102108-39-4 (2S,6S)-(E)-2-(cis-6-methyltetrahydropyran-2-yl)-1-phenylethene 
• 102208-93-5 (2R,6S)-(E)-2-(trans-6-methyltetrahydropyran-2-yl)-1-phenylethene 
• 102108-37-2 (7S)-(+)-3-acetoxy-1-phenyl-7-(tetrahydropyranyl-2-oxy)oct-1-ene 
• 102108-38-3 (7S)-(+)-3-acetoxy-7-hydroxy-1-phenyloct-1-ene 
• 102108-36-1 (7S)-(+)-3-hydroxy-1-phenyl-7-(tetrahydropyranyl-2-oxy)oct-1-ene 
• 102208-96-8 phenyl (2S,6S)-(cis-6-methyltetrahydropyran-2-yl)acetate 

Relevant academic research and scientific papers

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.