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Inhibition effects of furfural on alcohol dehydrogenase, aldehyde dehydrogenase and pyruvate dehydrogenase.

Modig, Tobias (author)
Lund University,Lunds universitet,Avdelningen för kemiteknik,Institutionen för processteknik och tillämpad biovetenskap,Institutioner vid LTH,Lunds Tekniska Högskola,Division of Chemical Engineering,Department of Process and Life Science Engineering,Departments at LTH,Faculty of Engineering, LTH,Dept. of Chemical Engineering II, Lund University
Lidén, Gunnar (author)
Lund University,Lunds universitet,Avdelningen för kemiteknik,Institutionen för processteknik och tillämpad biovetenskap,Institutioner vid LTH,Lunds Tekniska Högskola,Division of Chemical Engineering,Department of Process and Life Science Engineering,Departments at LTH,Faculty of Engineering, LTH,Dept. of Chemical Engineering II, Lund University
Taherzadeh, Mohammad J, 1965- (author)
Dept. of Chemical Engineering II, Lund University
 (creator_code:org_t)
2002
2002
English.
In: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 363:Pt 3, s. 769-776
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • The kinetics of furfural inhibition of the enzymes alcohol dehydrogenase (ADH; EC 1.1.1.1), aldehyde dehydrogenase (AlDH; EC 1.2.1.5) and the pyruvate dehydrogenase (PDH) complex were studied in vitro. At a concentration of less than 2 mM furfural was found to decrease the activity of both PDH and AlDH by more than 90%, whereas the ADH activity decreased by less than 20% at the same concentration. Furfural inhibition of ADH and AlDH activities could be described well by a competitive inhibition model, whereas the inhibition of PDH was best described as non-competitive. The estimated K(m) value of AlDH for furfural was found to be about 5 microM, which was lower than that for acetaldehyde (10 microM). For ADH, however, the estimated K(m) value for furfural (1.2 mM) was higher than that for acetaldehyde (0.4 mM). The inhibition of the three enzymes by 5-hydroxymethylfurfural (HMF) was also measured. The inhibition caused by HMF of ADH was very similar to that caused by furfural. However, HMF did not inhibit either AlDH or PDH as severely as furfural. The inhibition effects on the three enzymes could well explain previously reported in vivo effects caused by furfural and HMF on the overall metabolism of Saccharomyces cerevisiae, suggesting a critical role of these enzymes in the observed inhibition.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
TEKNIK OCH TEKNOLOGIER  -- Industriell bioteknik (hsv//swe)
ENGINEERING AND TECHNOLOGY  -- Industrial Biotechnology (hsv//eng)

Keyword

Binding
Competitive
Furaldehyde : pharmacology
Furaldehyde : analogs & derivatives
Models
Kinetics
Chemical
Pyruvate Dehydrogenase Complex : antagonists & inhibitors
Pyruvate Dehydrogenase Complex : metabolism
Pyruvic Acid : metabolism
Saccharomyces cerevisiae : enzymology
Aldehyde Dehydrogenase : antagonists & inhibitors
Alcohol Dehydrogenase : antagonists & inhibitors
A1DH

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Modig, Tobias
Lidén, Gunnar
Taherzadeh, Moha ...
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ENGINEERING AND TECHNOLOGY
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Lund University
University of Borås

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