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Studies of the Esterase Activity of Cytosolic Aldehyde Dehydrogenase Using Sterically Hindered and Cyclic Substrates

  • Kathryn E. Kitson
  • Treena J. Blythe
  • Trevor M. Kitson
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 372)

Abstract

Aldehyde dehydrogenase has the ability to catalyse the hydrolysis of p-nitrophenyl esters as well as the dehydrogenation of aldehydes by NAD+. Some work has been interpreted in terms of two different types of active site (Blackwell et al., 1983), but much other evidence points to the identity of the dehydrogenase and esterase sites (Loomes and Kitson, 1986; Kitson et al., 1991). In particular, Cys-302 has been identified as the nucleophile that becomes acylated by the aldehyde substrate trans-4-(N,N-dimethylamino)cinnamaldehyde (Pietruszko et al., 1993) and by the ester substrate analogue p-nitrophenyl dimethylcar-bamate (Kitson et al., 1991). Thus studying the esterase activity of aldehyde dehydrogenase should be capable of giving information about the active site of relevance to the dehydrogenase activity.

Keywords

Esterase Activity Aldehyde Dehydrogenase Ester Hydrolysis Affinity Matrix Vinyl Ketone 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Kathryn E. Kitson
    • 1
  • Treena J. Blythe
    • 1
  • Trevor M. Kitson
    • 1
  1. 1.Department of Chemistry and BiochemistryMassey UniversityPalmerston NorthNew Zealand

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