Kinetics and reaction mechanism of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae

Data from steady-state kinetic analysis of yeast K+-activated aldehyde dehydrogenase are consistent with a ternary complex mechanism. Evidence from alternative substrate analysis and product-inhibition studies supports an ordered sequence of substrate binding in which NAD+ is the leading substrate....

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Bibliographic Details
Published in:Biochemical journal 1978-09, Vol.173 (3), p.787-798
Main Authors: Bostian, K A, Betts, G F
Format: Article
Language:English
Subjects:
Aldehyde Oxidoreductases - antagonists & inhibitors
Aldehyde Oxidoreductases - metabolism
Enzyme Activation - drug effects
Kinetics
NAD
NADP
Potassium - pharmacology
Protein Binding
Saccharomyces cerevisiae - enzymology
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Summary:Data from steady-state kinetic analysis of yeast K+-activated aldehyde dehydrogenase are consistent with a ternary complex mechanism. Evidence from alternative substrate analysis and product-inhibition studies supports an ordered sequence of substrate binding in which NAD+ is the leading substrate. A preincubation requirement for NAD+ for maximum activity is also consistent with the importance of a binary enzyme-NAD+ complex. Dissociation constant for enzyme-NAD+ complex determined kinetically is in reasonable agreement with that determined by direct binding. The order of substrate addition proposed here differs from that proposed for a yeast aldehyde dehydrogenase previously reported. Different methods of purification produced an enzyme that showed similar kinetic characteristics to those reported here.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj1730787