Results 1 to 10 of about 104,574 (275)

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.
Raj SB, Ramaswamy S, Plapp BV.
europepmc   +5 more sources

Cytosolic re-localization and optimization of valine synthesis and catabolism enables inseased isobutanol production with the yeast Saccharomyces cerevisiae [PDF]

open access: yesBiotechnology for Biofuels, 2012
Background The branched chain alcohol isobutanol exhibits superior physicochemical properties as an alternative biofuel. The yeast Saccharomyces cerevisiae naturally produces low amounts of isobutanol as a by-product during fermentations, resulting from ...
Brat Dawid   +4 more
doaj   +3 more sources

Protein thermal stability in the undergraduate biochemistry laboratory: Exploring protein thermal stability with yeast alcohol dehydrogenase. [PDF]

open access: yesBiochem Mol Biol Educ
Abstract We created a novel laboratory experience where undergraduate students explore the techniques used to study protein misfolding, unfolding, and aggregation. Despite the importance of protein misfolding and aggregation diseases, protein unfolding is not typically explored in undergraduate biochemistry laboratory classes.
Bates A, Williams KM, Hagerman AE.
europepmc   +2 more sources

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.
Hans Jörnvall
semanticscholar   +3 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

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

open access: yesBiotechnology 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. Ward
semanticscholar   +3 more sources

Subunit conformation of yeast alcohol dehydrogenase.

open access: yesJournal of Biological Chemistry, 1978
The primary structure of yeast alcohol dehydrogenase has been compared to the known tertiary structure of the corresponding horse liver enzyme after proper alignment of the two proteins.
H. Jörnvall, H. Eklund, C. Brändén
semanticscholar   +3 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
semanticscholar   +3 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

Home - About - Disclaimer - Privacy