Alcohol dehydrogenase (ADH) in yeasts II. NAD+-and NADP+-dependent alcohol dehydrogenases inSaccharomycopsis lipolytica

1979 ◽  
Vol 19 (6) ◽  
pp. 381-390 ◽  
Author(s):  
G. Barth ◽  
W. Künkel
Keyword(s):  
Alcohol Dehydrogenase ◽  
Alcohol Dehydrogenases

scholarly journals An ADH toolbox for raspberry ketone production from natural resources via a biocatalytic cascade

2021 ◽  
Author(s):  
Aileen Becker ◽  
Dominique Böttcher ◽  
Werner Katzer ◽  
Karsten Siems ◽  
Lutz Müller-Kuhrt ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Genetically Modified Organisms ◽  
Optical Purity ◽  
High Yield ◽  
Alcohol Dehydrogenases ◽  
Flavor Compound ◽  
Raspberry Ketone ◽  
Cofactor Recycling ◽  
Cosmetic Industry ◽  
Key Points

Abstract Raspberry ketone is a widely used flavor compound in food and cosmetic industry. Several processes for its biocatalytic production have already been described, but either with the use of genetically modified organisms (GMOs) or incomplete conversion of the variety of precursors that are available in nature. Such natural precursors are rhododendrol glycosides with different proportions of (R)- and (S)-rhododendrol depending on the origin. After hydrolysis of these rhododendrol glycosides, the formed rhododendrol enantiomers have to be oxidized to obtain the final product raspberry ketone. To be able to achieve a high conversion with different starting material, we assembled an alcohol dehydrogenase toolbox that can be accessed depending on the optical purity of the intermediate rhododendrol. This is demonstrated by converting racemic rhododendrol using a combination of (R)- and (S)-selective alcohol dehydrogenases together with a universal cofactor recycling system. Furthermore, we conducted a biocatalytic cascade reaction starting from naturally derived rhododendrol glycosides by the use of a glucosidase and an alcohol dehydrogenase to produce raspberry ketone in high yield. Key points • LB-ADH, LK-ADH and LS-ADH oxidize (R)-rhododendrol • RR-ADH and ADH1E oxidize (S)-rhododendrol • Raspberry ketone production via glucosidase and alcohol dehydrogenases from a toolbox Graphical abstract

scholarly journals Further studies on the alcohol dehydrogenases in barley: evidence for a third alcohol dehydrogenase locus and data on the effect of an alcohol dehydrogenase – 1 null mutation in homozygous and in heterozygous condition

1983 ◽  
Vol 41 (2) ◽  
pp. 109-116 ◽  
Author(s):  
N. P. Harberd ◽  
K. J. R. Edwards
Keyword(s):  
Alcohol Dehydrogenase ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Null Mutation ◽  
Binomial Model ◽  
Wild Type ◽  
Alcohol Dehydrogenases ◽  
Heterozygous Condition ◽  
Adh Activity ◽  
Alcohol Dehydrogenase 1

SUMMARYThis paper presents evidence that the alcohol dehydrogenases (ADHs) in barley are specified by three loci. Six distinct ADH isozymes are observed following native slab polyacrylamide gel electrophoresis of crude extracts from flooded wild-type roots. Three of these isozymes are missing in flooded roots of plants homozygous for the Adhl-M9 mutation. The results also indicate that a simple binomial model (incorporating random dimerization and no inhibitive interaction of the two subunit species within heterodimers) is unable to account for the distribution of the total ADH activity between the ADH isozymes observed. Finally, the level and distribution of ADH activity in heterozygous (Adhl+ / Adhl-M9) flooded roots is not what would be expected if these contain only one-half of the available ADH1 protomers and the same frequency of available ADH2 and ADH3 protomers as is contained in the flooded roots of wild-type homozygotes (Adhl + / Adhl + ).

scholarly journals Variation in the Direction of Selection Applied by Pentenol to the Alcohol Dehydrogenase Locus in Drosophila melanogaster

1977 ◽  
Vol 30 (3) ◽  
pp. 259 ◽  
Author(s):  
JG Oakeshott
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Null Allele ◽  
Developmental Time ◽  
The Other ◽  
Laboratory Population ◽  
Alcohol Dehydrogenases ◽  
Alcohol Dehydrogenase Activity ◽  
Active Alcohol ◽  
Selective Effects

This paper describes selective effects of pentenol-impregnated media on six genotypes at the alcohol dehydrogenase (Adh) locus in D. melanogaster. In the laboratory population studied, developmental times of pre-adults homozygous for an alcohol dehydrogenase 'null' allele increased with increasing pentenol concentrations. The developmental times of the other five genotypes, which produced active alcohol dehydrogenases, increased slightly at pentenol concentrations up to 0�0033%, but above this concentration they decreased markedly. In fact on 0�067% pentenol, the highest concentration tested, developmental times of these five genotypes were between 9 and 24 h less than their developmental times on media lacking penteno!. The magnitude of the reduction in developmental time differed significantly between genotypes and was positively correlated with alcohol dehydrogenase activity.

scholarly journals A Pharmacophore-Based Approach to Demonstrating the Scope of Alcohol Dehydrogenases

2020 ◽  
Author(s):  
Katrina Madden ◽  
Peter M.T. Todd ◽  
Kouji Urata ◽  
Angela Russell ◽  
Kylie Vincent ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Screening Tool ◽  
Early Stage ◽  
Model Reaction ◽  
Screening Tools ◽  
High Tolerance ◽  
Alcohol Dehydrogenases ◽  
Ketone Reduction ◽  
Culture Shift ◽  
Chemical Groups

<p>Barriers to the ready adoption of biocatalysis into asymmetric synthesis for early stage medicinal chemistry are addressed, using ketone reduction by alcohol dehydrogenase as a model reaction. An efficient substrate screening approach is used to show the wide substrate scope of commercial alcohol dehydrogenase enzymes, with a high tolerance to chemical groups employed in drug discovery (heterocycle, trifluoromethyl and nitrile/nitro groups) observed. We use our screening data to build a preliminary predictive pharmacophore-based screening tool using Forge software, with a precision of 0.67/1, demonstrating the potential for developing substrate screening tools for commercially available enzymes without publically available structures. We hope that this work, combined with our simple protocols for scaleable H<sub>2</sub>-driven biocatalytic ketone reduction, will facilitate a culture shift towards adopting biocatalysis alongside traditional chemical catalytic methods.</p>

Conversion of Pyruvate Under Natural and Artificial Anaerobiosis in Maize

1976 ◽  
Vol 3 (6) ◽  
pp. 755 ◽  
Author(s):  
S Leblova ◽  
J Zima ◽  
E Perglerova
Keyword(s):  
Molecular Weight ◽  
Alcohol Dehydrogenase ◽  
Chelating Agents ◽  
Competitive Inhibitor ◽  
Cyclohexanone Oxime ◽  
Alcohol Dehydrogenases ◽  
Sh Groups ◽  
Competitive Inhibitors ◽  
Optimum Ph ◽  
Probable Presence

Lactate is formed during the initial hours of seed swelling during natural anaerobiosis in maize. Ethanol is formed later, at a concentration greater by one order. With 7-day-old seedlings, first lactate and then ethanol are also formed after transfer of the plants to an atmosphere of nitrogen. Lactate and alcohol dehydrogenases are active in the germinating seed. The molecular weight of maize alcohol dehydrogenase (EC 1.1.1.1) is 62 000 � 5000. Inhibition by chelating agents and 'sulphydryl poisons' indicates the probable presence of metal and -SH groups. The enzyme oxidizes ethanol at an optimum pH of 8.7 with a Km of 1.8 x 10-2 M and reduces acetaldehyde at an optimum pH of 6.7 with a Km of 1.0 x 10-3M. It is inhibited by succinate, malate, lactate and acetate, non-competitively with respect to the substrate. Acetoxime is a competitive inhibitor and butyrylamide, acetamide and cyclohexanone oxime are non-competitive inhibitors.

Regulation of NAD-specific alcohol dehydrogenases in Neurospora crassa

1969 ◽  
Vol 15 (3) ◽  
pp. 265-271 ◽  
Author(s):  
M. W. Zink
Keyword(s):  
Carbon Source ◽  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Neurospora Crassa ◽  
Sole Source ◽  
Protein Band ◽  
Alcohol Dehydrogenases

Neurospora crassa is capable of synthesizing two different alcohol dehydrogenases. The synthesis of each depends upon the carbon source on which the mycelium is grown. The fermentative alcohol dehydrogenase, consisting of one electrophoretic protein band, is produced when the mycelium is grown on sucrose. The oxidative alcohol dehydrogenase, consisting of at least two isozymes, is synthesized when Neurospora crassa is grown on ethanol as a sole source of carbon. This latter enzyme is repressed by sugars such as glucose or sucrose. The two enzymes have been differentiated (1) electrophoretically, (2) by their substrate specificity, (3) by the ratio of the forward and reverse reactions, and (4) by their thermostability. Extracts from acetate-grown cells indicate a mixture of the two enzymes.

scholarly journals The aromatic alcohol dehydrogenases in Pseudomonas putida N.C.I.B. 9869 grown on 3,5-xylenol and p-cresol

1978 ◽  
Vol 175 (2) ◽  
pp. 659-667 ◽  
Author(s):  
M J Keat ◽  
D J Hopper
Keyword(s):  
Alcohol Dehydrogenase ◽  
Pseudomonas Putida ◽  
The Other ◽  
Alcohol Dehydrogenases ◽  
Whole Cells ◽  
Aromatic Alcohol ◽  
Aromatic Alcohols ◽  
Hydroxybenzyl Alcohol

Whole cells of Pseudomonas putida N.C.I.B 9869, when grown on either 3,5-xylenol or p-cresol, oxidized both m- and p-hydroxybenzyl alcohols. Two distinct NAD+-dependent m-hydroxybenzyl alcohol dehydrogenases were purified from cells grown on 3,5-xylenol. Each is active with a range of aromatic alcohols, including both m- and p-hydroxybenzyl alcohol, but differ in their relative rates with the various substrates. An NAD+-dependent alcohol dehydrogenase was also partially purified from p-cresol grown cells. This too was active with m- and p-hydroxybenzyl alcohol and other aromatic alcohols, but was not identical with either of the other two dehydrogenases. All three enzymes were unstable, but were stabilized by dithiothreitol and all were inhibited with p-chloromercuribenzoate. All were specific for NAD+ and each was shown to catalyse conversion of alcohol into aldehyde.

scholarly journals Inhibition by ethanol, acetaldehyde and trifluoroethanol of reactions catalysed by yeast and horse liver alcohol dehydrogenases

1978 ◽  
Vol 171 (3) ◽  
pp. 613-627 ◽  
Author(s):  
C J Dickenson ◽  
F M Dickinson
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dissociation Constant ◽  
Maximum Rate ◽  
Alternative Pathway ◽  
Product Inhibition ◽  
Experimental Conditions ◽  
Alcohol Dehydrogenases ◽  
Yeast Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

1. Produced inhibition by ethanol of the acetaldehyde-NADH reaction, catalysed by the alcohol dehydrogenases from yeast and horse liver, was studied at 25 degrees C and pH 6-9. 2. The results with yeast alcohol dehydrogenase are generally consistent with the preferred-pathway mechanism proposed previously [Dickenson & Dickinson (1975) Biochem. J. 147, 303-311]. The observed hyperbolic inhibition by ethanol of the maximum rate of acetaldehyde reduction confirms the existence of the alternative pathway involving an enzyme-ethanol complex. 3. The maximum rate of acetaldehyde reduction with horse liver alcohol dehydrogenase is also subject to hyperbolic inhibition by ethanol. 4. The measured inhibition constants for ethanol provide some of the information required in the determination of the dissociation constant for ethanol from the active ternary complex. 5. Product inhibition by acetaldehyde of the ethanol-NAD+ reaction with yeast alcohol dehydrogenase was examined briefly. The results are consistent with the proposed mechanism. However, the nature of the inhibition of the maximum rate cannot be determined within the accessible range of experimental conditions. 6. Inhibition of yeast alcohol dehydrogenase by trifluoroethanol was studied at 25 degrees C and pH 6-10. The inhibition was competitive with respect to ethanol in the ethanol-NAD+ reaction. Estimates were made of the dissociation constant for trifluoroethanol from the enzyme-NAD+-trifluoroethanol complex in the range pH6-10.

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