Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to β-lactamase inhibitors |
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| Authors: | Thierry Brun,Jean Pé duzzi,Manuela Marin Caniç a,Gé rard Paul,Pierre Né vot,Michel Barthé lé my,Roger Labia |
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| Affiliation: | Department of Microbiology, University of Leeds, Leeds, LS2 9JT, UK; SmithKline Beecham Pharmaceuticals, Brockham Park, Betchworth, Surrey, RH3 7AJ, UK |
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| Abstract: | Abstract A novel procedure was used to purify a cytosolic chitinase from Candida albicans to electrophoretic homogeneity. The results represent the first demonstration of the purification of a fungal intracellular chitinase using the criterion of a single band detected following silver-staining of a polyacrylamide gel run under denaturing conditions. Purified chitinase had pH and temperature optima of 5.0 and 50°C, respectively. Inhibition of enzyme activity by allosamidin was pH-dependent occuring maximally at pH 8.0. Phospholipids had similar marked and highly specific effects on the activities of both the purified soluble enzyme and a solubilized microsomal chitinase from C. albicans . Evidence is provided for the existence of a complex chitinolytic system in this organism. |
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| Keywords: | Candida albicans Purified chitinase Phospholipid Complex chitinolytic system |
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