Design, synthesis, and biological evaluation of novel human 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP) substrates

Pei-Pei Kung; Luke R Zehnder; Jerry J Meng; Stanley W Kupchinsky; Donald J Skalitzky; M Catherine Johnson; Karen A Maegley; Anne Ekker; Leslie A Kuhn; Peter W Rose; Laura A Bloom

doi:10.1016/j.bmcl.2005.03.107

Design, synthesis, and biological evaluation of novel human 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP) substrates

Bioorg Med Chem Lett. 2005 Jun 2;15(11):2829-33. doi: 10.1016/j.bmcl.2005.03.107.

Authors

Pei-Pei Kung¹, Luke R Zehnder, Jerry J Meng, Stanley W Kupchinsky, Donald J Skalitzky, M Catherine Johnson, Karen A Maegley, Anne Ekker, Leslie A Kuhn, Peter W Rose, Laura A Bloom

Affiliation

¹ Pfizer Global Research and Development-La Jolla, San Diego, CA 92121, USA. peipei.kung@pfizer.com

PMID: 15911263
DOI: 10.1016/j.bmcl.2005.03.107

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).

MeSH terms

Drug Design
Humans
Molecular Structure
Purine-Nucleoside Phosphorylase / metabolism*
Substrate Specificity

Substances

Purine-Nucleoside Phosphorylase
5'-methylthioadenosine phosphorylase