A Molecular Mechanism of Hydrolysis of Peptide Bonds at Neutral pH Using a Model Compound

2011 ◽  
Vol 115 (19) ◽  
pp. 5958-5970 ◽  
Author(s):  
Bin Pan ◽  
Margaret S. Ricci ◽  
Bernhardt L. Trout
Keyword(s):  
Molecular Mechanism ◽  
Model Compound ◽  
Peptide Bonds ◽  
Neutral Ph ◽  
Mechanism Of Hydrolysis ◽  
Hydrolysis Of

scholarly journals TESTS FOR HYDROLYSIS OF PEPTIDE BONDS BY ULTRAVIOLET LIGHT

1950 ◽  
Vol 187 (2) ◽  
pp. 543-545
Author(s):  
Dorothy J. McLean ◽  
Arthur C. Giese
Keyword(s):  
Ultraviolet Light ◽  
Peptide Bonds ◽  
Hydrolysis Of

The Kinetics and Mechanism of Hydrolysis of Tetrachloroaurate(III)

1966 ◽  
Vol 5 (11) ◽  
pp. 1943-1946 ◽  
Author(s):  
Franklin H. Fry ◽  
Gordon A. Hamilton ◽  
John Turkevich
Keyword(s):  
Kinetics And Mechanism ◽  
Mechanism Of Hydrolysis ◽  
Hydrolysis Of

scholarly journals “Newton’s cradle” proton relay with amide–imidic acid tautomerization in inverting cellulase visualized by neutron crystallography

2015 ◽  
Vol 1 (7) ◽  
pp. e1500263 ◽  
Author(s):  
Akihiko Nakamura ◽  
Takuya Ishida ◽  
Katsuhiro Kusaka ◽  
Taro Yamada ◽  
Shinya Fushinobu ◽  
...  
Keyword(s):  
Glycoside Hydrolases ◽  
Side Chain ◽  
Enzymatic Reactions ◽  
X Ray Diffraction ◽  
Peptide Bonds ◽  
Proton Relay ◽  
Newton’S Cradle ◽  
Dynamics Simulations ◽  
Hydrolysis Of

Hydrolysis of carbohydrates is a major bioreaction in nature, catalyzed by glycoside hydrolases (GHs). We used neutron diffraction and high-resolution x-ray diffraction analyses to investigate the hydrogen bond network in inverting cellulase PcCel45A, which is an endoglucanase belonging to subfamily C of GH family 45, isolated from the basidiomycete Phanerochaete chrysosporium. Examination of the enzyme and enzyme-ligand structures indicates a key role of multiple tautomerizations of asparagine residues and peptide bonds, which are finally connected to the other catalytic residue via typical side-chain hydrogen bonds, in forming the “Newton’s cradle”–like proton relay pathway of the catalytic cycle. Amide–imidic acid tautomerization of asparagine has not been taken into account in recent molecular dynamics simulations of not only cellulases but also general enzyme catalysis, and it may be necessary to reconsider our interpretation of many enzymatic reactions.

Micellar catalysis of organic reactions. VIII. Kinetic studies of the hydrolysis of 2-acetyloxybenzoic acid (aspirin) in the presence of micelles

1982 ◽  
Vol 35 (7) ◽  
pp. 1357 ◽  
Author(s):  
TJ Broxton
Keyword(s):  
Aqueous Solution ◽  
Cetyltrimethylammonium Bromide ◽  
Cetylpyridinium Chloride ◽  
Kinetic Studies ◽  
Base Catalysis ◽  
Plateau Region ◽  
General Base ◽  
Mechanism Of Hydrolysis ◽  
Ph Range ◽  
Hydrolysis Of

The hydrolysis of 2-acetyloxybenzoic acid in the pH range 6-12 has been studied in the presence of micelles of cetyltrimethylammonium bromide (ctab) and cetylpyridinium chloride (cpc). In the plateau region (pH 6-8) the hydrolysis is inhibited by the presence of micelles, while in the region where the normal BAC2 hydrolysis (pH > 9) occurs the reaction is catalysed by micelles of ctab and cpc. The mechanism of hydrolysis in the plateau region is shown to involve general base catalysis by the adjacent ionized carboxy group both in the presence and absence of micelles. This reaction is inhibited in the presence of micelles because the substrate molecules are solubilized into the micelle and water is less available in this environment than in normal aqueous solution.

CZE–ICP-MS as a tool for studying the hydrolysis of ruthenium anticancer drug candidates and their reactivity towards the DNA model compound dGMP

2008 ◽  
Vol 102 (5-6) ◽  
pp. 1060-1065 ◽  
Author(s):  
Michael Groessl ◽  
Christian G. Hartinger ◽  
Paul J. Dyson ◽  
Bernhard K. Keppler
Keyword(s):  
Anticancer Drug ◽  
Model Compound ◽  
Drug Candidates ◽  
Icp Ms ◽  
Hydrolysis Of

The Effect of Dicarboxylic Acid Catalyst Structure on Hydrolysis of Cellulose Model Compound D-Cellobiose in Water

2021 ◽  
Vol 08 ◽  
Author(s):  
Harshica Fernando ◽  
Ananda S. Amarasekara
Keyword(s):  
Dicarboxylic Acid ◽  
Model Compound ◽  
Acid Catalyst ◽  
Catalytic Activities ◽  
Polycarboxylic Acids ◽  
Hydrolysis Of Cellulose ◽  
Phthalic Acids ◽  
Turn Over Frequency ◽  
Turn Over ◽  
Hydrolysis Of

Background: Polycarboxylic acids are of interest as simple mimics for cellulase enzyme catalyzed depolymerization of cellulose. In this study, DFT calculations were used to investigate the effect of structure on dicarboxylic acid organo-catalyzed hydrolysis of cellulose model compound D-cellobiose to D-glucose. Methods: Binding energy of the complex formed between D-cellobiose and acid (Ebind), as well as glycosidic oxygen to dicarboxylic acid closest acidic H distance were studied as key parameters affecting the turn over frequency of hydrolysis in water. Result: α-D-cellobiose - dicarboxylic acid catalyst down face approach showed high Ebind values for five of the six acids studied; indicating the favorability of down face approach. Maleic, cis-1,2-cyclohexane dicarboxylic, and phthalic acids with the highest catalytic activities showed glycosidic oxygen to dicarboxylic acid acidic H distances 3.5-3.6 Å in the preferred configuration. Conclusion: The high catalytic activities of these acids may be due to the rigid structure, where acid groups are held in a fixed geometry.

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