Journal
CURRENT DRUG TARGETS
Volume 13, Issue 4, Pages 512-525Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138945012799499730
Keywords
Catalytic mechanism; drug discovery; glycosyl hydrolase; inhibition; structure; target; pesticide
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Funding
- National Key Project for Basic Research [2010CB126100]
- National Natural Science Foundation of China [31070715, 31101671]
- National High Technology Research and Development Program of China [2011AA10A204]
- National Key Technology RD Program [2011BAE06B05]
- Fundamental Research Funds for the Central Universities [DUT11ZD113]
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Glycosyl hydrolase family 3, 20 and 84 beta-N-acetyl-D-hexosaminidases are widely distributed enzymes that function in energy metabolism, cell proliferation, signal transduction as well as in pathogen-related inflammation and autoimmune diseases. Sharing the same retaining catalytic mechanism, they are distinguished from each other in terms of structure rather than substrate-enzyme transition state. Selective inhibition of each of these enzymes that exploits the structural differences would appear promising in the regulation and investigation of their corresponding life functions within the organism. Thanks to molecular structural biology, detailed structures of GH3, 20 and 84 beta-N-acetyl-D-hexosaminidases have become available at the atomic level. This review gives a panoramic description and comparison of the enzymes catalytic mechanisms, overall structures, active site architectures as well as structure-based analysis of inhibition, with the hope of exploiting novel targets for developing novel drugs and pesticides.
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