Properties of adenosine monophosphate deaminase of Candida albicans.
Adenosine monophosphate deaminase (AMPD; EC 3.5.4.6) catalyses the hydrolysis of adenosine monophosphate (AMP) to commensurate amounts of inosine monophosphate (IMP) and ammonia. The production of AMP deaminase in Candida albicans was measured in Lee's medium grown cultures. The highest AMPD activity was observed at 24 h of growth. The enzyme had an optimum pH and temperature at 6-7 and 28 degrees C, respectively. This enzyme was inhibited under iron-limited growth conditions as well as by protease inhibitors. The AMPD of C. albicans showed a moderate increase in activity when cultures were grown in the presence of the divalent cations Mg2+, Ca2+, and Zn2+. Moreover, ADP, ATP, adenine, adenosine, deoxyribose and hypoxanthine increased the enzyme activity. Cultures grown in trypticase soy broth exhibited maximum AMPD activity compared with those grown in Sabouraud dextrose broth or Lee's medium.
Thompson
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Department of Biology, Fisk University, Nashville, Tennessee 37208, USA.
Hall
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Karunakaran
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Gunasekaran
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D000659:AMP Deaminase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000249:Adenosine Monophosphate / Q000378:metabolism; D002176:Candida albicans / Q000201:enzymology* / Q000254:growth & development; D003470:Culture Media / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D011480:Protease Inhibitors / Q000494:pharmacology; D013696:Temperature; D013997:Time Factors
D003470:Culture Media; D011480:Protease Inhibitors; D000249:Adenosine Monophosphate; D000659:AMP Deaminase