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 <scene name='59/595220/Cv/2'>5’-deoxy-5’-methylthioadenosine (MTA)</scene> to adenine and 5-methylthio-D-ribose-1-phosphate. <scene name='59/595220/Cv/4'>Click here to see active site</scene>. 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.<ref>PMID:10404592</ref> | '''5’-deoxy-5’-methylthioadenosine phosphorylase''' (MTAP) catalyzes the reversible phosphorolysis of <scene name='59/595220/Cv/2'>5’-deoxy-5’-methylthioadenosine (MTA)</scene> to adenine and 5-methylthio-D-ribose-1-phosphate. <scene name='59/595220/Cv/4'>Click here to see active site</scene> (PDB code [[1cg6]]). <ref>PMID:10404592</ref> 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.<ref>PMID:10404592</ref> | ||
== Disease == | == Disease == |
Revision as of 14:15, 13 December 2015
Function5’-deoxy-5’-methylthioadenosine phosphorylase (MTAP) catalyzes the reversible phosphorolysis of to adenine and 5-methylthio-D-ribose-1-phosphate. (PDB code 1cg6). [1] 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.[2] DiseaseMTAP is deficient in many cancers because it is co-deleted with the tumor suppressor p16. RelevanceMTAP is a potential target of chemotherapy. More than 20% of human various cancer cells do not show MTAP activity.
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3D structures of 5’-deoxy-5’-methylthioadenosine phosphorylase3D structures of 5’-deoxy-5’-methylthioadenosine phosphorylase
Updated on 13-December-2015
ReferencesReferences
- ↑ 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
- ↑ 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