The Low Barrier Hydrogen Bond in Enzymatic Catalysis
Open Access
- 1 October 1998
- journal article
- review article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (40) , 25529-25532
- https://doi.org/10.1074/jbc.273.40.25529
Abstract
No abstract availableThis publication has 46 references indexed in Scilit:
- NMR Studies of the Role of Hydrogen Bonding in the Mechanism of Triosephosphate IsomeraseBiochemistry, 1997
- Theoretical Study of the Low-Barrier Hydrogen Bond in the Hydrogen Maleate Anion in the Gas Phase. Comparison with Normal Hydrogen BondsJournal of the American Chemical Society, 1997
- A Very Short Hydrogen Bond Provides Only Moderate Stabilization of an Enzyme-Inhibitor Complex of Citrate SynthaseBiochemistry, 1994
- Low-Barrier Hydrogen Bonds and Enzymic CatalysisScience, 1994
- A Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine ProteasesScience, 1994
- The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: Mechanistic and crystallographic evidence for stereospecific alkylation by (R)-.alpha.-phenylglycidateBiochemistry, 1994
- Understanding the rates of certain enzyme-catalyzed reactions: Proton abstraction from carbon acids, acyl transfer reactions, and displacement reactions of phosphodiestersBiochemistry, 1993
- On the interaction of 2-keto-3-deoxygalactonate-6P with 2-keto-3-deoxygluconate-6P aldolase ofPseudomonas putida. Evidence for enzyme-mediated, noncatalytic C-C bond turnoverProtein Journal, 1983
- 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