Human cytidine deaminase: understanding the catalytic mechanism.
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.
Costanzi
S
S
Dipartimento di Scienze Chimiche, University of Camerino, Camerino, Italy. stefano.costanzi@unicam.it
Vincenzetti
S
S
Vita
A
A
Lambertucci
C
C
Taffi
S
S
Volpini
R
R
Vittori
S
S
Cristalli
G
G
D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D003564:Cytidine Deaminase / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
D029968:Escherichia coli Proteins; D021122:Protein Subunits; D003564:Cytidine Deaminase