Abstract
Summary Alcohol oxidase is irreversibly inactivated by the acetylenic substrates propargyl alcohol and 1,4-butynediol. In both cases, inactivation results from affinity labeling of amino acid residues in the active site of the enzyme by propynal and 4-hydroxy-2-butynal, the electrophilic products of the oxidation of these alcohols. The inactivation by 4-hydroxy-2-butynal occurs with the aldehyde bound in the active site of the enzyme in the orientation which is opposite to that in which it had been produced. Alcohol oxidase is inactivated by acetylenic substrates in a fundamentally different manner than are the formally similar flavin-dependent α-hydroxy acid oxidases.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
