salivary aldehyde dehydrogenase activity towards aromatic aldehydes and comparison with recombinant aldh3a1唾液醛脱氢酶活性与重组aldh3a1芳香醛和比较.pdfVIP

Molecules 2009, 14, 2363-2372; doi:10.3390/molecule OPEN ACCESS molecules ISSN 1420-3049 /journal/molecules Article Salivary Aldehyde Dehydrogenase: Activity towards Aromatic Aldehydes and Comparison with Recombinant ALDH3A1 1 2 3 3 Joanna Giebułtowicz , Renata Wolinowska , Anna Sztybor , Monika Pietrzak , Piotr Wroczyński 1 and Jacek Wierzchowski 3,* 1 Department of Drugs Analysis, Faculty of Pharmacy, Medical University of Warsaw, 1 Banacha Street, PL-02-097, Warsaw, Poland; E-mail: joanna.giebultowicz@ (J.G.) 2 Department of Pharmaceutical Microbiology, Faculty of Pharmacy, Medical University of Warsaw, 3 Oczki Street, PL-02-007, Warsaw, Poland; E-mail: rwolinowska@.pl (R.W.) 3 Department of Biophysics, University of Warmia and Mazury, 4 Oczapowskiego St., PL-10-719 Olsztyn, Poland * Author to whom correspondence should be addressed; E-mail: jacek.wie@.pl; Tel. +48-89-523-3324; Fax: +48-89-523-3408 Received: 11 May 2009; in revised form: 15 June 2009 / Accepted: 18 June 2009 / Published: 2 July 2009 Abstract: 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 onl