5'-deoxy-5'-methylthioadenosine phosphorylase: Difference between revisions
Jump to navigation
Jump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
Line 3: | Line 3: | ||
== 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/3'>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. | '''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/3'>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> | ||
== Disease == | == Disease == |
Revision as of 13:34, 3 December 2015
Function5’-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] 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.
|
|
3D structures of 5’-deoxy-5’-methylthioadenosine phosphorylase3D structures of 5’-deoxy-5’-methylthioadenosine phosphorylase
Updated on 03-December-2015