title: Design, synthesis, and biological evaluation of novel human 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP) substrates.
abstract: The structure-based design, chemical synthesis, and biological evaluation of novel MTAP substrates are described. These compounds incorporate various C5'-moieties and are shown to have different k(cat)/K(m) values compared with the natural MTAP substrate (MTA).
authors.affiliation: Pfizer Global Research and Development-La Jolla, San Diego, CA 92121, USA. peipei.kung@pfizer.com
authors.forename: Pei-Pei
authors.initials: PP
authors.lastname: Kung
authors.forename: Luke R
authors.initials: LR
authors.lastname: Zehnder
authors.forename: Jerry J
authors.initials: JJ
authors.lastname: Meng
authors.forename: Stanley W
authors.initials: SW
authors.lastname: Kupchinsky
authors.forename: Donald J
authors.initials: DJ
authors.lastname: Skalitzky
authors.forename: M Catherine
authors.initials: MC
authors.lastname: Johnson
authors.forename: Karen A
authors.initials: KA
authors.lastname: Maegley
authors.forename: Anne
authors.initials: A
authors.lastname: Ekker
authors.forename: Leslie A
authors.initials: LA
authors.lastname: Kuhn
authors.forename: Peter W
authors.initials: PW
authors.lastname: Rose
authors.forename: Laura A
authors.initials: LA
authors.lastname: Bloom
mesh_terms: D015195:Drug Design; D006801:Humans; D015394:Molecular Structure; D011683:Purine-Nucleoside Phosphorylase / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D011683:Purine-Nucleoside Phosphorylase; C021784:5'-methylthioadenosine phosphorylase