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Studies on thermal stability of human cytidine deaminase
- Source :
- Nucleosides, nucleotidesnucleic acids. 26(8-9)
- Publication Year :
- 2007
-
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.
- Subjects :
- Circular dichroism
Stereochemistry
In Vitro Techniques
Biochemistry
chemistry.chemical_compound
Catalytic Domain
Cytidine Deaminase
Enzyme Stability
Genetics
Humans
Thermal stability
Protein Structure, Quaternary
chemistry.chemical_classification
Circular Dichroism
Cytidine
General Medicine
Cytidine deaminase
Recombinant Proteins
Glutamine
Enzyme
chemistry
Amino Acid Substitution
Drug Design
Glycine
Pyrimidine metabolism
Mutagenesis, Site-Directed
Molecular Medicine
Thermodynamics
Subjects
Details
- ISSN :
- 15257770
- Volume :
- 26
- Issue :
- 8-9
- Database :
- OpenAIRE
- Journal :
- Nucleosides, nucleotidesnucleic acids
- Accession number :
- edsair.doi.dedup.....e005d9a6e19e1bb48c0a347906f2cd3e