5'-deoxy-5'-methylthioadenosine phosphorylase

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. 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.

spinqualitylabelsall models Structure of human MTAP complex with MTA (PDB code 1cg6). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Updated on 22-October-2015

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• MTAP
  • 3oze – hMTAP - human
    
  • 4glf – ubMTAP – uncultured bacteria
    
  • 4l5y – SmMTAP – Schistosoma mansoni
    
  • 1jp7, 1jpv – SsMTAP – Sulfolobus solfataricus
    
• MTAP complex with adenine
  • 1cb0 – hMTAP (mutant) + adenine
    
  • 1wta – MTAP + adenine – Aeropyrum pernix
    
  • 4l5c, 4l6i – SmMTAP + adenine
    
• MTAP complex with MTA
  • 1cg6 – hMTAP (mutant) + MTA
    
  • 2a8y, 3t94 – SsMTAP + MTA
    
• MTAP complex with antibiotics
  • 1sd1, 1sd2 – hMTAP + antibiotic
    
  • 4l5a – SmMTAP + antibiotic
    
• MTAP other complexes
  • 3ozc, 3ozd – hMTAP + pCL-phenylthioDADMeImmA
    
  • 4glj – ubMTAP + rhodamine
    
  • 1k27 – hMTAP + transition state analog