Mode of Action of Bi- and Trinuclear Zinc Hydrolases and Their Synthetic Analogues
Top Cited Papers
- 24 March 2005
- journal article
- review article
- Published by American Chemical Society (ACS) in Chemical Reviews
- Vol. 105 (6) , 2151-2174
- https://doi.org/10.1021/cr020057z
Abstract
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This publication has 332 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Structural determinants and hydrogen-bond network of the mononuclear zinc(II)-β-lactamase active siteJBIC Journal of Biological Inorganic Chemistry, 2002
- Artificial Evolution of an Enzyme Active Site: Structural Studies of Three Highly Active Mutants of Escherichia coli Alkaline PhosphataseJournal of Molecular Biology, 2002
- A revised mechanism for the alkaline phosphatase reaction involving three metal ionsJournal of Molecular Biology, 2000
- The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 å resolution 1 1Edited by K. NagaiJournal of Molecular Biology, 1998
- Macrocyclic zinc(II) complexes for selective recognition of nucleobases in single- and double-stranded polynucleotidesJBIC Journal of Biological Inorganic Chemistry, 1998
- Crystal Structure of Phospholipase C from Bacillus cereus Complexed with a Substrate AnalogJournal of Molecular Biology, 1993
- Crystal structures of phosphate, iodide and iodate-inhibited phospholipase C from Bacillus cereus and structural investigations of the binding of reaction products and a substrate analogueJournal of Molecular Biology, 1992
- Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatinJournal of Molecular Biology, 1992
- Refined structure of alkaline phosphatase from Escherichia coli at 2.8 Å resolutionJournal of Molecular Biology, 1985