Human cytidine deaminase: understanding the catalytic mechanism.

S Costanzi, S Vincenzetti, A Vita, C Lambertucci, S Taffi, R Volpini, S Vittori, G Cristalli

Journal: Nucleosides, nucleotides & nucleic acids 2003;22(5-8):1539-43

PMID: 14565461

Abstract

In the absence of an experimentally elucidated three-dimensional structure of the human CDA, we built an homology model of this enzyme starting from the crystal structure of its E. coli homologous. Furthermore, we docked in the active site alternatively the substrate, the intermediate or the product. By means of molecular dynamics simulations, we determined the topology of the active site, identifying the amino acids involved in the catalytic mechanism, and outlining the central role played by E67.

Address: Dipartimento di Scienze Chimiche, University of Camerino, Camerino, Italy. [email protected]

DOI: 10.1081/NCN-120023029

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MeSH Terms: Amino Acid Sequence, Binding Sites, Catalysis, Cytidine Deaminase, Escherichia coli, Escherichia coli Proteins, Humans, Models, Molecular, Protein Conformation, Protein Structure, Secondary, Protein Subunits