title: [Theoretical study of antagonists and inhibitors of mammalian adenosine deaminase. II. Isomeric aza-deazaanalogues of adenosine].
abstract: Isomeric aza-deazaanalogues of adenosine and their N1-protonated forms (except for that of 8-aza-1-deazaadenosine) were studied by computer modeling to find a relationship between their molecular structures and the properties as substrates for the mammalian adenosine deaminase. The atomic charge distribution and maps of the electrostatic potential around their van der Waals molecular surface were calculated using the ab initio STO-3G method. The conformational studies were carried out by the MM+ method of molecular mechanics. The previously proposed mechanism of the substrate acceptance in the active site of mammalian adenosine deaminase was refined, and the potential substrate properties were predicted for two previously unstudied adenosine analogues, 5-aza-9-deazaadenosine and 8-aza-3-deazaadenosine.
authors.affiliation: Department of Organic Chemistry, Samara State University, ul. Akademika Pavlova 1, Samara, 443011 Russia. zarubin@ssu.samara.ru
authors.forename: Iu P
authors.initials: IuP
authors.lastname: Zarubin
authors.forename: I A
authors.initials: IA
authors.lastname: Il'icheva
authors.forename: P P
authors.initials: PP
authors.lastname: Purygin
authors.forename: V L
authors.initials: VL
authors.lastname: Florent'ev
mesh_terms: D000241:Adenosine / Q000031:analogs & derivatives* / Q000737:chemistry*; D058892:Adenosine Deaminase Inhibitors; D000818:Animals; D004791:Enzyme Inhibitors / Q000737:chemistry*; D007536:Isomerism; D008322:Mammals; D008958:Models, Molecular; D008962:Models, Theoretical; D009690:Nucleic Acid Conformation; D013379:Substrate Specificity
chemical_list: D058892:Adenosine Deaminase Inhibitors; D004791:Enzyme Inhibitors; D000241:Adenosine