5'-deoxy-5'-methylthioadenosine phosphorylase

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== Function ==
== Function ==
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'''5’-deoxy-5’-methylthioadenosine phosphorylase''' (MTAP) catalyzes the reversible phosphorolysis of <scene name='59/595220/Cv/7'>5’-deoxy-5’-methylthioadenosine (MTA)</scene> to adenine and 5-methylthio-D-ribose-1-phosphate. <scene name='59/595220/Cv/6'>Click here to see active site</scene> (PDB code [[1cg6]]). 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>
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'''5’-deoxy-5’-methylthioadenosine phosphorylase''' (MTAP) catalyzes the reversible phosphorolysis of <scene name='59/595220/Cv/7'>5’-deoxy-5’-methylthioadenosine (MTA)</scene> to adenine and 5-methylthio-D-ribose-1-phosphate. <scene name='59/595220/Cv/6'>Click here to see active site</scene> (PDB code [[1cg6]]). Water molecule is shown as red sphere. 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 13:47, 28 October 2019

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

Drag the structure with the mouse to rotate


References

  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

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