The thermal stability of human cytidine deaminase (CDA), an enzyme involved in pyrimidine metabolism was investigated. With this in view, the residues R68 and Y60, supposed to be involved in the intersubunit interactions and in the catalytic site of CDA, were mutated to glutamine and glycine, respectively. Thermal stability experiments were performed on the purified mutants by means of circular dichroism and enzymatic assays. The results obtained should be useful for designing more efficient cytidine based drugs for chemotherapy.

Studies on thermal stability of human cytidine deaminase

VINCENZETTI, Silvia;PUCCIARELLI, Stefania;DE SANCTIS, Giampiero;POLZONETTI, Valeria;NATALINI, Paolo;VITA, Alberto
2007-01-01

Abstract

The thermal stability of human cytidine deaminase (CDA), an enzyme involved in pyrimidine metabolism was investigated. With this in view, the residues R68 and Y60, supposed to be involved in the intersubunit interactions and in the catalytic site of CDA, were mutated to glutamine and glycine, respectively. Thermal stability experiments were performed on the purified mutants by means of circular dichroism and enzymatic assays. The results obtained should be useful for designing more efficient cytidine based drugs for chemotherapy.
2007
262
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11581/114189
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