Chitinase activity from Candida albicans and its inhibition by allosamidin.
Candida albicans chitinase isolated using the Dyno-Mill disruption technique was characterized using an improved radiometric assay procedure. The enzyme had apparent temperature and pH optima of 45 degrees C and 6.5, respectively. The preparation yielded an apparent Km of 3.9 mg chitin ml-1 [17.6 mM-N-acetylglucosamine (GlcNAc) equivalents] and V of 2.3 nmol GlcNAc formed min-1 (mg protein)-1. The potential of the streptomycete antibiotic allosamidin as an antifungal agent is discussed in view of its dose-dependent inhibition of C. albicans chitinase activity (IC50 = 0.3 microM). Allosamidin was a potent competitive inhibitor of enzyme activity (Ki = 0.23 microM).
Dickinson
K
K
Department of Microbiology, University of Leeds, UK.
Keer
V
V
Hitchcock
C A
CA
Adams
D J
DJ
D000117:Acetylglucosamine / Q000031:analogs & derivatives* / Q000494:pharmacology; D002176:Candida albicans / Q000201:enzymology*; D002686:Chitin / Q000378:metabolism; D002688:Chitinases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D005656:Fungal Proteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D005944:Glucosamine / Q000031:analogs & derivatives*; D006863:Hydrogen-Ion Concentration; D008828:Microbiological Techniques; D013696:Temperature; D014312:Trisaccharides
D005656:Fungal Proteins; D014312:Trisaccharides; C054851:allosamidin; D002686:Chitin; D002688:Chitinases; D005944:Glucosamine; D000117:Acetylglucosamine