5'-deoxy-5'-methylthioadenosine phosphorylase

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Function

5’-deoxy-5’-methylthioadenosine phosphorylase (MTAP) catalyzes the reversible phosphorolysis of to adenine and 5-methylthio-D-ribose-1-phosphate. . MTAP is part of the polyamine metabolism. This reaction is the principle source of adenine in human cells. MTAP catalyzes the first step in the methionine salvage pathway.[1]

Disease

MTAP is deficient in many cancers because it is co-deleted with the tumor suppressor p16.

Relevance

MTAP is a potential target of chemotherapy. More than 20% of human various cancer cells do not show MTAP activity.


Structure of human MTAP complex with MTA and sulfate (PDB code 1cg6).

Drag the structure with the mouse to rotate

3D structures of 5’-deoxy-5’-methylthioadenosine phosphorylase3D structures of 5’-deoxy-5’-methylthioadenosine phosphorylase

Updated on 03-December-2015

ReferencesReferences

  1. Appleby TC, Erion MD, Ealick SE. The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis. Structure. 1999 Jun 15;7(6):629-41. PMID:10404592

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman