A Catalytic Diad Involved in Substrate-Assisted Catalysis: NMR Study of Hydrogen Bonding and Dynamics at the Active Site of Phosphatidylinositol-Specific Phospholipase C
- 18 July 2001
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 40 (32) , 9743-9750
- https://doi.org/10.1021/bi010958m
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Substrate‐assisted catalysis: Molecular basis and biological significanceProtein Science, 2000
- Identification of a Novel Catalytic Triad with Dual Functions in Enzymatic Cleavage of the P−O BondJournal of the American Chemical Society, 1998
- Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenesJournal of Molecular Biology, 1997
- Synthesis, Structure−Activity Relationships, and the Effect of Polyethylene Glycol on Inhibitors of Phosphatidylinositol-Specific Phospholipase C fromBacillus cereusJournal of Medicinal Chemistry, 1996
- Toward the mechanism of phosphoinositide-specific phospholipases CBioorganic & Medicinal Chemistry, 1994
- Exchangeable proton NMR without base-line distorsion, using new strong-pulse sequencesJournal of the American Chemical Society, 1982
- Observation of histidine residues in proteins by nuclear magnetic resonance spectroscopyAccounts of Chemical Research, 1975
- High resolution nuclear magnetic resonance studies of the active site of chymotrypsin: II. Polarization of histidine 57 by substrate analogues and competitive inhibitorsJournal of Molecular Biology, 1974
- High resolution nuclear magnetic resonance study of the histidine—Aspartate hydrogen bond in chymotrypsin and chymotrypsinogenJournal of Molecular Biology, 1972
- Proton Transfer, Acid‐Base Catalysis, and Enzymatic Hydrolysis. Part I: ELEMENTARY PROCESSESAngewandte Chemie International Edition in English, 1964