5'-deoxy-5'-methylthioadenosine phosphorylase: Difference between revisions

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== Function ==
== Function ==


'''5’-deoxy-5’-methylthioadenosine phosphorylase''' (MTAP)  catalyzes the reversible phosphorolysis of 5’-deoxy-5’-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate.  This reaction is the principle source of adenine in human cells.
'''5’-deoxy-5’-methylthioadenosine phosphorylase''' (MTAP)  catalyzes the reversible phosphorolysis of 5’-deoxy-5’-methylthioadenosine (MTA) 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.


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


== Relevance ==
== Relevance ==

Revision as of 12:31, 21 October 2015


Function

5’-deoxy-5’-methylthioadenosine phosphorylase (MTAP) catalyzes the reversible phosphorolysis of 5’-deoxy-5’-methylthioadenosine (MTA) 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.

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.

Structural highlights

Structure of human MTAP complex with MTA (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 21-October-2015

ReferencesReferences

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

Michal Harel, Alexander Berchansky, Joel L. Sussman