Purification and characterization of l-allo-threonine aldolase from Aeromonas jandaei DK-39 |
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Authors: | Michihiko Kataokaa Masaru Wadaa Ken-ichi Nishia Hideaki Yamadaa Sakayu Shimizua |
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Institution: | Department of Public Health, Pharmacology and Toxicology, Faculty of Veterinary Medicine, University of Nairobi, P.O. Box 29053, Nairobi, Kenya;Institut für Genetik und Mikrobiologie, Universität München, Maria Ward Str. 1a, D-80638 Munich, Germany |
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Abstract: | l-allo-Threonine aldolase (l-allo-threonine acetaldehyde-lyase), which exhibited specificity for l-allo-threonine but not for l-threonine, was purified from a cell-free extract of Aeromonas jandaei DK-39. The purified enzyme catalyzed the aldol cleavage reaction of l-allo-threonine (Km=1.45 mM, Vmax=45.2 μmol min?1 mg?1). The activity of the enzyme was inhibited by carbonyl reagents, which suggests that pyridoxal-5′-phosphate participates in the enzymatic reaction. The enzyme does not act on either l-serine or l-threonine, and thus it can be distinguished from serine hydroxy-methyltransferase (l-serine:tetrahydrofolate 5,10-hydroxy-methyltransferase, EC 2.1.2.1) or l-threonine aldolase (EC 4.1.2.5). |
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Keywords: | Bacillus cereus Enterotoxin Polymerase chain reaction Hybridization |
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