Results 11 to 20 of about 1,029 (146)

Immobilization and stabilization of alcohol dehydrogenase on polyvinyl alcohol fibre [PDF]

Biotechnology Reports, 2018
A polyvinyl alcohol (PVA) fibrous carrier has been chemically modified for the immobilization of yeast alcohol dehydrogenase (ADH) with an aim to increase its stability over a wide pH range, prolong its activity upon storage, and enhance its reusability.
Priydarshani Shinde, Mustafa Musameh, Yuan Gao, Andrea J. Robinson, Ilias (Louis) Kyratzis   +4 more
doaj   +3 more sources

Functional characterization of SlscADH1, a fruit-ripening associated short-chain alcohol dehydrogenase of tomato [PDF]

, 2012
A tomato short-chain dehydrogenase-reductase (SlscADH1) is preferentially expressed in fruit with a maximum expression at the breaker stage while expression in roots, stems, leaves and flowers is very weak.
Moummou, Hanane, Chervin, Christian, Latché, Alain, Pech, Jean-Claude, Benichou, Mohamed, Tonfack, Libert Brice, Ginies, Christian, Van der Rest, Benoît, Youmbi, Emmanuel   +8 more
core   +1 more source

Glycerol dehydrogenase: Structure, specificity, and mechanism of a family III polyol dehydrogenase [PDF]

, 2001
Background: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) (glycerol:NAD+ 2-oxidoreductase, EC 1.1.1.6) catalyzes the oxidation of glycerol to dihydroxyacetone (1,3-dihydroxypropanone) with concomitant reduction of NAD+ to NADH.
Baker PJ, Sveta Sedelnikova, Taylor R, Sedelnikova S, Baker, Patrick J., Rice DW, Muir, Nicola M., Gore, Michael G., Burke J, David W. Rice, Ruzheinikov, Sergey N., Bullough, Per A., Sedelnikova, Sveta, Sergey N. Ruzheinikov, Per A. Bullough, Patrick J. Baker, Gore MG, Burke, Jacky, Michael G. Gore, Muir NM, Bullough PA, Nicola M. Muir, Rice, David W., Robert Taylor, Ruzheinikov SN, Jacky Burke, Taylor, Robert   +26 more
core   +1 more source

Yeast Alcohol Dehydrogenase Structure and Catalysis [PDF]

Biochemistry, 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. A structure for ADH1 was determined by X-ray crystallography at 2.4 Å resolution. The asymmetric unit contains four different
Raj, Savarimuthu Baskar, Ramaswamy, S., Plapp, Bryce V.   +2 more
openaire   +2 more sources

Aromatic aldehydes as substrates for yeast and yeast alcohol dehydrogenase [PDF]

Biotechnology and Bioengineering, 1989
We have investigated the conversion of aromatic aldehydes to L-acetyl aromatic carbinols and aromatic alcohols by Saccharomyces cerevisiae and also the conversion of aldehyde to corresponding alcohol by yeast alcohol ...
A, Long, P, James, O P, Ward
openaire   +2 more sources

Inhibition of alcohol dehydrogenase from yeast by pyridine [PDF]

Biochemical Journal, 1967
1. Inhibition by pyridine of reduction of NAD by ethanol in the presence of yeast alcohol dehydrogenase was studied at 25 degrees in 60mm-glycine buffer (K(+), pH9.3). 2. The apparent Michaelis constant for ethanol increases linearly and that for NAD increases non-linearly with pyridine concentration. 3.
M R, Atkinson, G, Eckermann, R M, Lilley
openaire   +2 more sources

ALDH2 mediates 5-nitrofuran activity in multiple species [PDF]

, 2012
Understanding how drugs work in vivo is critical for drug design and for maximizing the potential of currently available drugs. 5-nitrofurans are a class of pro-drugs widely used to treat bacterial and trypanosome infections, but despite relative ...
Spitzer, Michaela, Brear, Paul, Patton, E. Elizabeth, Johnson, Stephen L, Patton, E Elizabeth, Zeng, Zhiqiang, Patton, Elizabeth, Mitchell, Amy, Ishizaki, Hironori, Taylor, Kerrie L, Johnson, Stephen L., Taylor, Kerrie L., Smith, Terry K., Westwood, Nicholas J, Patton, E Elizabeth; id_orcid, Marie, K.L.; id_orcid, McNeil, Ewan, Temperley, Nicholas, Tyers, Mike, Melton, David W, Zhou, Linna, Temperley, Nicholas D., Temperley, Nicholas D, Gautier, Philippe, Taylor, Kerrie, Narayan, Vikram, Melton, David, Westwood, Nicholas James, Melton, David W., Smith, Terry K, Johnson, Stephen, McNeil, Ewan M, McNeil, Ewan M., Westwood, Nicholas J.   +33 more
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Coupled oxidation–reduction of butanol–hexanal by resting Rhodococcus erythropolis NCIMB 13064 cells in liquid and gas phases [PDF]

, 2008
Rhodococcus erythropolis is a promising Gram-positive bacterium capable of numerous bioconversions including those involving alcohol dehydrogenases (ADHs).
Rosenfeld, Eric, Maugard, T., Marchand, Pierre, Marchand, P., Erable, Benjamin, Rosenfeld, E., Maugard, Thierry, Goubet, I., Goubet, Isabelle, Lamare, Sylvain, Lamare, S.   +10 more
core   +1 more source

Identification of an NADH-dependent 5-hydroxymethylfurfural-reducing alcohol dehydrogenase in Saccharomyces cerevisiae. [PDF]

, 2008
We report on the identification and characterization of a mutated alcohol dehydrogenase 1 from the industrial Saccharomyces cerevisiae strain TMB3000 that mediates the NADH-dependent reduction of 5-hydroxymethylfurfural (HMF) to 2,5-bis ...
João R. M. Almeida, Laadan, Boaz, Rådström, Peter, Peter Rådström, Almeida, Joao, Gorwa-Grauslund, Marie-Francoise,, Hahn-Hägerdal, Bärbel, Boaz Laadan, Marie Gorwa‐Grauslund, Gorwa-Grauslund, Marie-Francoise, Bärbel Hahn‐Hägerdal   +10 more
core   +1 more source

Studies on the biosynthesis of cholesterol: XIV. the origin of prenoic acids from allyl Pyrophosphates in liver enzyme systems

Journal of Lipid Research, 1961
Allyl pyrophosphates (3,3-dimethylallyl, geranyl, and farnesyl pyrophosphate), which are known intermediates in the biosynthesis of squalene from mevalonate, are also metabolized in the liver by an alternative pathway to acids.
J. Christophe, G. Popják
doaj   +1 more source