Results 31 to 40 of about 1,338,228 (382)

Relation entre les difficultés de fermentation et certaines activités enzymatiques de la levure

open access: yesOENO One, 1984
The arrest of fermentation in medium rich in sugar (grape must) is not related to the inhibition of hexokinase and alcohol-dehydrogenase activities of Sacch. cerevisiae.
Françoise Larue   +2 more
doaj   +1 more source

Yeast Alcohol Dehydrogenase Structure and Catalysis

open access: yesBiochemistry, 2014
Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues.
S. B. Raj, S. Ramaswamy, B. Plapp
semanticscholar   +1 more source

Erratum [PDF]

open access: yesJournal of the Serbian Chemical Society, 2000
Erratum In the paper entitled "Structure and Function of Yeast Alcohol Dehydrogenase" by Svetlana Trivić and Vladimir Leskovac published in J. Serb. Chem. Soc. Vol. 65. No. 4 (2000) Table 5 on page 213 should be replaced with: TABLE V.
Editorial
doaj   +1 more source

Structure and function of yeast alcohol dehydrogenase [PDF]

open access: yesJournal of the Serbian Chemical Society, 2000
1. Introduction 2. Isoenzymes of YADH 3. Substrate specificity 4. Kinetic mechanism 5. Primary structure 6. The active site 7. Mutations in the yeast enzyme 8. Chemical mechanism 9. Binding of coenzymes 10.
Trivić Svetlana, Leskovac Vladimir
doaj   +3 more sources

Prokaryotic 20β-hydroxysteroid dehydrogenase is an enzyme of the ‘short-chain, non-metalloenzyme’ alcohol dehydrogenase type [PDF]

open access: yes, 1990
The primary structure of 20β-hydroxysteroid dehydrogenase from Streptomyces hydrogenans was determined after FPLC purification of a commercial preparation. Peptides obtained from different proteolytic cleavages were purified by reverse phase HPLC.
Jörnvall, Hans   +2 more
core   +1 more source

Knockout of secondary alcohol dehydrogenase in Nocardia cholesterolicum NRRL 5767 by CRISPR/Cas9 genome editing technology.

open access: yesPLoS ONE, 2020
Nocardia cholesterolicum NRRL 5767 is well-known for its ability to convert oleic acid to 10-hydroxystearic acid (~88%, w/w) and 10-ketostearic acid (~11%, w/w).
Jenq-Kuen Huang   +8 more
doaj   +1 more source

High blood alcohol levels in women. The role of decreased gastric alcohol dehydrogenase activity and first-pass metabolism.

open access: yesNew England Journal of Medicine, 1990
After consuming comparable amounts of ethanol, women have higher blood ethanol concentrations than men, even with allowance for differences in size, and are more susceptible to alcoholic liver disease.
M. Frezza   +5 more
semanticscholar   +1 more source

Alcohol dehydrogenase and aldehyde dehydrogenase genotypes and alcoholism among Taiwanese aborigines [PDF]

open access: yesBiological Psychiatry, 1997
Previous population association studies have indicated that certain alleles of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) genes may reduce the risk of alcoholism in Oriental populations. In this report we determined the genotypes for three genes, ADH2, ADH3, and ALDH2 among subjects with alcohol dependence (n = 159) and ethnically ...
Chen, Wei J.   +3 more
openaire   +3 more sources

Multiple alcohol dehydrogenases but no functional acetaldehyde dehydrogenase causing excessive acetaldehyde production from ethanol by oral streptococci.

open access: yesMicrobiology, 2013
Ethanol consumption and poor oral hygiene are risk factors for oral and oesophageal cancers. Although oral streptococci have been found to produce excessive acetaldehyde from ethanol, little is known about the mechanism by which this carcinogen is ...
S. Pavlova   +3 more
semanticscholar   +1 more source

The oxygen-independent metabolism of cyclic monoterpenes in Castellaniella defragrans 65Phen [PDF]

open access: yes, 2014
BACKGROUND: The facultatively anaerobic betaproteobacterium Castellaniella defragrans 65Phen utilizes acyclic, monocyclic and bicyclic monoterpenes as sole carbon source under oxic as well as anoxic conditions.
Becher, D.   +7 more
core   +2 more sources

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