Studies on thermal stability of human cytidine deaminase.
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.
Dipartimento di Scienze Morfologiche e Biochimiche Comparate, Università di Camerino, Camerino, Italy. silvia.vincenzetti@unicam.it
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S
Vincenzetti
S
S
Pucciarelli
P
P
Mariani
G
G
De Sanctis
V
V
Polzonetti
P
P
Natalini
A
A
Vita
D019943:Amino Acid Substitution; D020134:Catalytic Domain; D002942:Circular Dichroism; D003564:Cytidine Deaminase / Q000737:chemistry* / Q000235:genetics; D015195:Drug Design; D004795:Enzyme Stability; D006801:Humans; D066298:In Vitro Techniques; D016297:Mutagenesis, Site-Directed; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013816:Thermodynamics
D011994:Recombinant Proteins; D003564:Cytidine Deaminase