Two mitochondrial alcohol dehydrogenase activities of Kluyveromyces lactis are differently expressed during respiration and fermentation

1995 ◽  
Vol 249 (6) ◽  
pp. 665-672 ◽  
Author(s):  
Michele Saliola ◽  
Claudio Falcone
Keyword(s):  
Alcohol Dehydrogenase ◽  
Kluyveromyces Lactis

The alcohol dehydrogenase system in the yeast,Kluyveromyces lactis

Yeast ◽  
1990 ◽  
Vol 6 (3) ◽  
pp. 193-204 ◽  
Author(s):  
Michele Saliola ◽  
Jeffrey R. Shuster ◽  
Claudio Falcone
Keyword(s):  
Alcohol Dehydrogenase ◽  
Kluyveromyces Lactis ◽  
Dehydrogenase System

Structural and biochemical studies of alcohol dehydrogenase isozymes from Kluyveromyces lactis

1997 ◽  
Vol 1339 (1) ◽  
pp. 133-142 ◽  
Author(s):  
Argante Bozzi ◽  
Michele Saliola ◽  
Claudio Falcone ◽  
Francesco Bossa ◽  
Filippo Martini
Keyword(s):  
Alcohol Dehydrogenase ◽  
Kluyveromyces Lactis ◽  
Biochemical Studies

Kinetic properties of native and mutagenized isoforms of mitochondrial alcohol dehydrogenase III purified from Kluyveromyces lactis

Biochimie ◽  
2004 ◽  
Vol 86 (9-10) ◽  
pp. 705-712 ◽  
Author(s):  
Fabrizia Brisdelli ◽  
Michele Saliola ◽  
Stefano Pascarella ◽  
Carla Luzi ◽  
Nicola Franceschini ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Kluyveromyces Lactis ◽  
Kinetic Properties ◽  
Alcohol Dehydrogenase Iii

scholarly journals Pichia stipitis Genes for Alcohol Dehydrogenase with Fermentative and Respiratory Functions

1998 ◽  
Vol 64 (4) ◽  
pp. 1350-1358 ◽  
Author(s):  
Jae-yong Cho ◽  
Thomas W. Jeffries
Keyword(s):  
Alcohol Dehydrogenase ◽  
Kluyveromyces Lactis ◽  
Pichia Stipitis ◽  
Amino Acid Sequences ◽  
Aerobic Growth ◽  
Lower Growth ◽  
Amino Terminal ◽  
Group I ◽  
Lower Growth Rate ◽  
High Level

ABSTRACT Two genes coding for isozymes of alcohol dehydrogenase (ADH); designated PsADH1 and PsADH2, have been identified and isolated from Pichia stipitis CBS 6054 genomic DNA by Southern hybridization to Saccharomyces cerevisiae ADH genes, and their physiological roles have been characterized through disruption. The amino acid sequences of the PsADH1 and PsADH2 isozymes are 80.5% identical to one another and are 71.9 and 74.7% identical to the S. cerevisiae ADH1 protein. They also show a high level identity with the group I ADH proteins fromKluyveromyces lactis. The PsADH isozymes are presumably localized in the cytoplasm, as they do not possess the amino-terminal extension of mitochondrion-targeted ADHs. Gene disruption studies suggest that PsADH1 plays a major role in xylose fermentation becausePsADH1 disruption results in a lower growth rate and profoundly greater accumulation of xylitol. Disruption ofPsADH2 does not significantly affect ethanol production or aerobic growth on ethanol as long as PsADH1 is present. The PsADH1 and PsADH2 isozymes appear to be equivalent in the ability to convert ethanol to acetaldehyde, and either is sufficient to allow cell growth on ethanol. However, disruption of both genes blocks growth on ethanol. P. stipitis strains disrupted in eitherPsADH1 or PsADH2 still accumulate ethanol, although in different amounts, when grown on xylose under oxygen-limited conditions. The PsADH double disruptant, which is unable to grow on ethanol, still produces ethanol from xylose at about 13% of the rate seen in the parental strain. Thus, deletion of both PsADH1 and PsADH2 blocks ethanol respiration but not production, implying a separate path for fermentation.

Multiple unfolded states of alcohol dehydrogenase I from Kluyveromyces lactis by guanidinium chloride

2001 ◽  
Vol 1545 (1-2) ◽  
pp. 238-244 ◽  
Author(s):  
Paolo Sacchetta ◽  
Rosalba Di Rado ◽  
Michele Saliola ◽  
Argante Bozzi ◽  
Claudio Falcone ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Kluyveromyces Lactis ◽  
Guanidinium Chloride
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