Preparative-scale reductions of cyclic ketones and aldehyde substrates of horse liver alcohol dehydrogenase with in situ sodium dithionite recycling of catalytic amounts of NAD

1972 ◽  
pp. 856 ◽  
Author(s):  
J. Bryan Jones ◽  
David W. Sneddon ◽  
William Higgins ◽  
Arthur J. Lewis
Keyword(s):  
Alcohol Dehydrogenase ◽  
Sodium Dithionite ◽  
Cyclic Ketones ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Preparative Scale ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

Enzymes in organic synthesis. 32. Stereospecific horse liver alcohol dehydrogenase-catalyzed oxidations of exo- and endo-oxabicyclic meso diols

1984 ◽  
Vol 62 (11) ◽  
pp. 2578-2582 ◽  
Author(s):  
J. Bryan Jones ◽  
Christopher J. Francis
Keyword(s):  
Alcohol Dehydrogenase ◽  
Organic Synthesis ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Preparative Scale ◽  
Enantiomerically Pure ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
One Step ◽  
Catalyzed Oxidation ◽  
Enzymes In Organic Synthesis

Preparative-scale horse liver alcohol dehydrogenase-catalyzed oxidation of mesoexo- and endo-7-oxabicyclo[2.2.1]heptane diols provides a direct one-step route to enantiomerically pure chiral γ-lactones of the oxabicyclic series.

Enzymes in organic syntheses. 19. Evaluation of the stereoselectivities of horse liver alcohol dehydrogenase; catalyzed oxidoreductions of hydroxy- and ketothiolanes, -thianes, and -thiepanes

1981 ◽  
Vol 59 (11) ◽  
pp. 1574-1579 ◽  
Author(s):  
J. Bryan Jones ◽  
Harold M. Schwartz
Keyword(s):  
Alcohol Dehydrogenase ◽  
Membered Ring ◽  
Oxidation Reactions ◽  
Structural Variations ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Preparative Scale ◽  
Scale Reduction ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Reduction And Oxidation

The specificity of horse liver alcohol dehydrogenase (HLADH) with respect to unsubstituted five-, six-, and seven-membered ring 3- and 4-thiaketone and -thiaalcohol substrates has been examined. The enzyme is found to have a broad tolerance of the structural variations within this series. HLADH also exhibits encouraging (up to 46%) enantiotopic and enantiomeric specificity in preparative-scale reduction and oxidation reactions of the heterocyclic ketones and alcohols respectively.

Regiospecific horse liver alcohol dehydrogenase-catalyzed oxidations of some bishydroxycyclohexanes

1977 ◽  
Vol 55 (14) ◽  
pp. 2685-2691 ◽  
Author(s):  
J. Bryan Jones ◽  
H. Bruce Goodbrand
Keyword(s):  
Alcohol Dehydrogenase ◽  
Secondary Alcohol ◽  
Primary Alcohol ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Preparative Scale ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

Horse liver alcohol dehydrogenase has been shown to be effective in catalyzing regiospecific oxidations of only the primary alcohol functions of several cyclohexane substrates possessing both primary and secondary alcohol substituents. The reactions, which were all performed on a preparative scale, were also enantioselective in some cases.

Enzymes in organic synthesis. 14. Stereoselective horse liver alcohol dehydrogenase catalyzed oxidations of diols containing a prochiral centre and of related hemiacetals

1979 ◽  
Vol 57 (9) ◽  
pp. 1025-1032 ◽  
Author(s):  
J. Bryan Jones ◽  
Kar P. Lok
Keyword(s):  
Alcohol Dehydrogenase ◽  
Organic Synthesis ◽  
Initial Oxidation ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Catalyzed Oxidation ◽  
Enzymes In Organic Synthesis ◽  
Hydroxyethyl Group

The asymmetric synthetic potential of horse liver alcohol dehydrogenase catalyzed oxidations of variously 3-substituted pentane-1,5-diols has been further delineated. The oxidations proceed with enantiotopic selectivity to give the corresponding (3S)-3-substituted valerolactones of up to 78% ee. The reactions occur via initial oxidation of the pro-S hydroxyethyl group, with the initially-formed hydroxyaldehydes undergoing further in situ enzyme-catalyzed oxidation in their hemiacetal forms to give the (3S)-lactones directly. The hemiacetal oxidation step is also stereoselective, with oxidation of the (4S)-enantiomer being much preferred. The size of the substituent at C-3 in the diols (C-4 in the hemiacetals) affects both the enantiotopic and enantiomeric specificity of the enzyme. Both types of stereospecificity are highest when the substituents are smallest, such as methyl or ethyl, and diminish progressively for diol or hemiacetal substrates bearing large aliphatic or aromatic substituents. All reactions were carried out on a preparative (up to 2 g) scale.

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