Salivary Aldehyde Dehydrogenase: Activity towards Aromatic Aldehydes and Comparison with Recombinant ALDH3A1

Molecules

Joanna Giebułtowicz¹  Renata Wolinowska³  Anna Sztybor²  Monika Pietrzak²  Piotr Wroczyński¹ 

[1] Department of Drugs Analysis, Faculty of Pharmacy, Medical University of Warsaw, 1 Banacha Street, PL-02-097, Warsaw, Poland; E-mail:;Department of Biophysics, University of Warmia and Mazury, 4 Oczapowskiego St., PL-10-719 Olsztyn, Poland;Department of Pharmaceutical Microbiology, Faculty of Pharmacy, Medical University of Warsaw, 3 Oczki Street, PL-02-007, Warsaw, Poland; E-mail:

关键词: saliva;    aldehyde dehydrogenase;    enzyme kinetics;    aromatic aldehydes;   

DOI  :  10.3390/molecules14072363

来源: mdpi

【 摘 要 】

A series of aromatic aldehydes was examined as substrates for salivary aldehyde dehydrogenase (sALDH) and the recombinant ALDH3A1. Para-substituted benzaldehydes, cinnamic aldehyde and 2-naphthaldehydes were found to be excellent substrates, and kinetic parameters for both salivary and recombinant ALDH were nearly identical. It was demonstrated that for the fluorogenic naphthaldehydes the only produced reaction product after incubation in saliva is the carboxylate.

【 授权许可】

CC BY   
© 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.