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Yeast alcohol dehydrogenase structure and catalysis. [PDF]

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. A structure for ADH1 was determined by X-ray crystallography at 2.4 Å resolution. The asymmetric unit contains four different
Raj SB, Ramaswamy S, Plapp BV.
europepmc   +4 more sources

High-Throughput Screening of Industrial Brewing Yeast with Lower Synthetic Level of Acetaldehyde During Beer Production [PDF]

open access: yesFoods
The high level of acetaldehyde produced by yeast is a significant concern for all enterprises of beer production. To obtain industrial beer yeast strains with low ability to produce acetaldehyde, a multi-step screening strategy was established, using ...
Shuangxin Han   +9 more
doaj   +2 more sources

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

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

Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalysed 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 ºC, have been estimated. The determination of the individual rate constants was achieved by fitting the
Leskovac Vladimir M.   +2 more
doaj   +1 more source

Recombinant yeast for production of the pain receptor modulator nonivamide from vanillin

open access: yesFrontiers in Chemical Engineering, 2023
We report on the development of a method based on recombinant yeast Saccharomyces cerevisiae to produce nonivamide, a capsaicinoid and potent agonist of the pain receptor TRPV1. Nonivamide was produced in a two-step batch process where yeast was i) grown
Nina Muratovska, Magnus Carlquist
doaj   +1 more source

MAGNETIC FIELD EFFECT ON YEAST Saccharomyces cerevisiae ACTIVITY AT GRAPE MUST FERMENTATION [PDF]

open access: yesBiotechnologia Acta, 2013
Treatment of yeast cultures using magnetic fields enables us to gain a better understanding of the magnetic fields’ action on enzyme activity and the fluctuation of macro- and micro-element concentrations within yeast cultures.
V. N. Bayraktar
doaj   +1 more source

High-throughput screening for growth inhibitors using a yeast model of familial paraganglioma. [PDF]

open access: yesPLoS ONE, 2013
Classical tumor suppressor genes block neoplasia by regulating cell growth and death. A remarkable puzzle is therefore presented by familial paraganglioma (PGL), a neuroendocrine cancer where the tumor suppressor genes encode subunits of succinate ...
Irina Bancos   +12 more
doaj   +1 more source

Effects of the Addition of Dendrobium officinale on Beer Yeast Fermentation

open access: yesFermentation, 2022
Dendrobium officinale is a precious Chinese medicinal plant that is rich in polysaccharides, flavonoids, polyphenols, and other bioactive ingredients, and has a variety of biological activities. To explore the effects of D.
Xiaolu Chen   +3 more
doaj   +1 more source

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

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