HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Bradbury, S. L. Articles by Jakoby, W. B. Search for Related Content PubMed PubMed Citation Articles by Bradbury, S. L. Articles by Jakoby, W. B. Social Bookmarking                      What's this?

Ordered Binding of Substrates to Yeast Aldehyde Dehydrogenase

From the ¹ From the Section on Enzymes and Cellular Biochemistry, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014

Yeast aldehyde dehydrogenase catalyzes the pyridine nucleotide-linked oxidation of a broad range of aldehydes to the corresponding acids. The reaction is experimentally irreversible. Initial velocity studies with DPN and two different aldehyde substrates, and equilibrium dialysis experiments with DPN, indicate that the substrates bind in a compulsory order; aldehyde and enzyme interact to make a binary complex which, in turn, forms a ternary complex with DPN. The equilibrium dialysis experiments were complicated by the ubiquitous presence of contaminating aldehydes and were made possible by the inclusion of a DPN-regenerating system. DPNH behaves as a competitive inhibitor of DPN and combines only with the enzyme aldehyde complex. Since neither of the pyridine nucleotides forms a binary complex with enzyme, the data fit a model in which aldehyde binds first while acid dissociates last.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?