Results 31 to 40 of about 25,112 (256)

The reactions of 1,10-phenanthroline with yeast alcohol dehydrogenase [PDF]

open access: yesBiochemical Journal, 1977
Freshly prepared samples of yeast alcohol dehydrogenase (EC 1.1.1.1) were inhibited by 1,10-phenanthroline at pH 7.0 and 0 degrees C in a two-stage process. The first step appeared to be slowly established, but was rendered reversible by removal of reagent or by addition of excess Zn2+ ions.
F M, Dickinson, S, Berrieman
openaire   +2 more sources

Stereoselective Biotransformation: Transfer of Learning to Advance Drug Metabolism and Biocatalysis

open access: yesAngewandte Chemie, EarlyView.
Understanding stereoselective biotransformations has implications for predicting drug disposition and response and may also inspire novel biocatalytic and biomimetic strategies to address challenges in metabolite and API synthesis. ABSTRACT Chirality is an important determinant of drug action, as enantiomers can exhibit markedly different ...
Grace A. Okunlola, Godwin A. Aleku
wiley   +2 more sources

Substrate specificities of peroxisomal members of short-chain alcohol dehydrogenase superfamily: expression and characterization of dehydrogenase part of Candida tropicalismultifunctional enzyme

open access: yesJournal of Lipid Research, 2000
In addition to several other enzymes, the short-chain alcohol dehydrogenase superfamily includes a group of peroxisomal multifunctional enzymes involved in fatty acid and cholesterol side-chain β-oxidation.
Yong-Mei Qin   +2 more
doaj   +1 more source

The Primary Structure of Yeast Alcohol Dehydrogenase [PDF]

open access: yesEuropean Journal of Biochemistry, 1977
Eight different types of peptide mixtures from [14C]carboxymethylated yeast alcohol dehydrogenase were obtained using trypsin with or without prior maleylation of the substrate, chymotrypsin, pepsin, microbial proteases or CNBr. Each mixture was fractionated by exclusion chromatography and peptides were further purified on paper.
openaire   +2 more sources

The Two Major Isozymes of Yeast Alcohol Dehydrogenase [PDF]

open access: yesEuropean Journal of Biochemistry, 1979
The structures of the two cytoplasmic isozymes of alcohol dehydrogenase in a haploid strain of the yeast Saccharomyces cerevisiae have been compared and related to a commercial preparation of the protein that was previously analyzed. The constitutive isozyme I (purified from a petite cell incapable of mitochondrial respiration) is found to correspond ...
C, Wills, H, Jörnvall
openaire   +2 more sources

Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalyzed reactions [PDF]

open access: yesJournal of the Serbian Chemical Society, 2003
In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD+, at pH 7.0, 25°C, have been estimated.
DRAGINJA PERICIN   +2 more
doaj  

Genome and transcriptome analysis of the food-yeast Candida utilis. [PDF]

open access: yesPLoS ONE, 2012
The industrially important food-yeast Candida utilis is a Crabtree effect-negative yeast used to produce valuable chemicals and recombinant proteins. In the present study, we conducted whole genome sequencing and phylogenetic analysis of C. utilis, which
Yasuyuki Tomita   +4 more
doaj   +1 more source

Inhibition of Yeast Alcohol Dehydrogenase by Alkylating Agents [PDF]

open access: yesEuropean Journal of Biochemistry, 1968
1 The kinetic parameters for the irreversible inhibition of yeast alcohol dehydrogenase by iodoacetate, bromopyruvate and N-ethylmaleimide have been measured. 2 For iodoacetate and bromopyruvate, the rate of inhibition decreases with increasing pH. It is concluded that the reaction is promoted by a positive centre on the enzyme with a pKa value of
N, Rashed, B R, Rabin
openaire   +2 more sources

Resurrecting ancestral alcohol dehydrogenases from yeast [PDF]

open access: yesNature Genetics, 2005
Modern yeast living in fleshy fruits rapidly convert sugars into bulk ethanol through pyruvate. Pyruvate loses carbon dioxide to produce acetaldehyde, which is reduced by alcohol dehydrogenase 1 (Adh1) to ethanol, which accumulates. Yeast later consumes the accumulated ethanol, exploiting Adh2, an Adh1 homolog differing by 24 (of 348) amino acids.
J Michael, Thomson   +6 more
openaire   +2 more sources

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

open access: yes, 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   +26 more
core   +1 more source

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