Structural Comparison of MTA Phosphorylase and MTA/AdoHcy Nucleosidase Explains Substrate Preferences and Identifies Regions Exploitable for Inhibitor Design

Medicine & Life Sciences

• adenosylhomocysteine nucleosidase 100%
• 5'-methylthioadenosine phosphorylase 82%
• N-Glycosyl Hydrolases 62%
• Pemetrexed 61%
• Phosphorylases 24%
• 5'-methylthiotubercidin 10%
• formycin 8%
• Binding Sites 6%
• Ribose 5%
• Quorum Sensing 5%
• Sequence Alignment 5%
• Polyamines 5%
• Adenine 5%
• Static Electricity 5%
• purine 4%
• Recycling 4%
• Drug Design 4%
• Substrate Specificity 4%
• Enzymes 4%
• Methionine 4%
• Metabolic Networks and Pathways 4%
• Methylation 3%
• Mammals 3%
• Poisons 3%
• Escherichia coli 2%
• Pharmaceutical Preparations 1%
• Therapeutics 0%

Chemical Compounds

• Thioribose 51%
• Formycin A 42%
• Antiprotozoal Agent 38%
• Binding Site 33%
• Ribose 26%
• Polyamine 25%
• Electrostatic Potential 24%
• Purine 23%
• Byproduct 23%
• Adenine 21%
• Recycling 21%
• Biosynthesis 19%
• Metabolic 19%
• Toxic 17%
• Catalysis 15%
• Drug 12%
• Crystal Structure 11%