Biosynthesis of mitochondrial proteins in the cytoplasm and their transport to the mitochondrial membrane [PDF]
Neupert, Walter
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The oleaginous yeast Cutaneotrichosporon oleaginosum modifies corn stover alkali lignin. [PDF]
Gluth A +9 more
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Comparative genomics of dominant members of the gut core microbiome of the bark beetle, Dendroctonus rhizophagus (Curculionidae: Scolytinae) reveals potential functional complementarity in the detoxification process. [PDF]
Vazquez-Ortiz K +2 more
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High-yield production of hydroxytyrosol through metabolic engineering of <i>Yarrowia lipolytica</i>. [PDF]
Chen B +6 more
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Engineering energy-efficient Saccharomyces cerevisiae for methanol and CO<sub>2</sub> assimilation. [PDF]
Zhong W +8 more
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Co-Fermentation with <i>Lactiplantibacillus plantarum</i> and <i>Pichia pastoris</i>: A Novel Approach to Enhance Flavor and Quality of Fermented Tea Beverage. [PDF]
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Advances in microbial mevalonolactone production: from fermentative mevalonate accumulation to downstream lactonization. [PDF]
Tang H +7 more
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Production of yeast alcohol dehydrogenase isoenzymes by selection
Nature, 1976Mutants of yeast alcohol dehydrogenase have been produced that protect the cell against the poisonous aldehyde acrolein by increasing the NADH-NAD ratio. The altered properties include changes both in binding constants and in cooperativity. Such mutants may be useful in exploring the nature of adaptation at the molecular level.
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Cryo-Electron Microscopy Structures of Yeast Alcohol Dehydrogenase.
Biochemistry, 2021Structures of yeast alcohol dehydrogenase determined by X-ray crystallography show that the subunits have two different conformational states in each of the two dimers that form the tetramer.
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Borate inhibition of yeast alcohol dehydrogenase.
Biochemistry, 1976Yeast alcohol dehydrogenase is inhibited competitively by borate with respect to NAD+. An unusual mechanism of competitive inhibition prevails: the competition for the substrate NAD+ by borate and enzyme. The following evidence supports this conclusion. (1) Much greater inhibition is observed with respect to NAD+ as compared with NADH as substrates. (2)
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