Design, synthesis, and biological evaluation of novel human 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP) substrates.
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).
Kung
Pei-Pei
PP
Pfizer Global Research and Development-La Jolla, San Diego, CA 92121, USA. peipei.kung@pfizer.com
Zehnder
Luke R
LR
Meng
Jerry J
JJ
Kupchinsky
Stanley W
SW
Skalitzky
Donald J
DJ
Johnson
M Catherine
MC
Maegley
Karen A
KA
Ekker
Anne
A
Kuhn
Leslie A
LA
Rose
Peter W
PW
Bloom
Laura A
LA
D015195:Drug Design; D006801:Humans; D015394:Molecular Structure; D011683:Purine-Nucleoside Phosphorylase / Q000378:metabolism*; D013379:Substrate Specificity
D011683:Purine-Nucleoside Phosphorylase; C021784:5'-methylthioadenosine phosphorylase