A Case for Reverse Protonation:  Identification of Glu160 as an Acid/Base Catalyst inThermoanaerobacterium saccharolyticumβ-Xylosidase and Detailed Kinetic Analysis of a Site-Directed Mutant†

Biochemistry ◽  
2002 ◽  
Vol 41 (31) ◽  
pp. 9736-9746 ◽  
Author(s):  
David J. Vocadlo ◽  
Jacqueline Wicki ◽  
Karen Rupitz ◽  
Stephen G. Withers
Keyword(s):  
Kinetic Analysis ◽  
Base Catalyst ◽  
Acid Base ◽  
A Site ◽  
Reverse Protonation

Identification of the Acid/Base Catalyst in Agrobacterium faecalis .beta.-Glucosidase by Kinetic Analysis of Mutants

Biochemistry ◽  
1995 ◽  
Vol 34 (44) ◽  
pp. 14554-14562 ◽  
Author(s):  
Q. Wang ◽  
D. Trimbur ◽  
R. Graham ◽  
R. A. J. Warren ◽  
S. G. Withers
Keyword(s):  
Kinetic Analysis ◽  
Base Catalyst ◽  
Acid Base ◽  
Beta Glucosidase

Cesium-modified hollow ZSM-5: efficient acid-base catalyst for side-chain alkylation of 2-picoline with formaldehyde

2021 ◽  
pp. 117983
Author(s):  
Zhe Hong ◽  
Guoqing Zhao ◽  
Chuanfang Xiong ◽  
Wenzhi Jia ◽  
Fangtang Huang ◽  
...  
Keyword(s):  
Side Chain ◽  
Base Catalyst ◽  
Acid Base

scholarly journals Trigger loop of RNA polymerase is a positional, not acid–base, catalyst for both transcription and proofreading

2017 ◽  
pp. 201702383 ◽  
Author(s):  
Tatiana V. Mishanina ◽  
Michael Z. Palo ◽  
Dhananjaya Nayak ◽  
Rachel A. Mooney ◽  
Robert Landick
Keyword(s):  
Rna Polymerase ◽  
Base Catalyst ◽  
Acid Base ◽  
Trigger Loop

The Acid/Base Catalyst in the Exoglucanase/Xylanase from Cellulomonas fimi Is Glutamic Acid 127: Evidence from Detailed Kinetic Studies of Mutants

Biochemistry ◽  
1994 ◽  
Vol 33 (20) ◽  
pp. 6371-6376 ◽  
Author(s):  
Alasdair M. MacLeod ◽  
Thisbe Lindhorst ◽  
Stephen G. Withers ◽  
R. Antony J. Warren
Keyword(s):  
Glutamic Acid ◽  
Kinetic Studies ◽  
Base Catalyst ◽  
Acid Base ◽  
Cellulomonas Fimi

scholarly journals Can an Alcohol Act As an Acid/Base Catalyst in Water Solution? An Experimental and Theoretical Study of Imidazole Catalysis of the Aqueous Morita–Baylis–Hillman Reaction

ACS Catalysis ◽  
2018 ◽  
Vol 8 (3) ◽  
pp. 1703-1714 ◽  
Author(s):  
Lluís Raich ◽  
Hugo Santos ◽  
Juliana C. Gomes ◽  
Manoel T. Rodrigues ◽  
Renan Galaverna ◽  
...  
Keyword(s):  
Theoretical Study ◽  
Water Solution ◽  
Base Catalyst ◽  
Acid Base ◽  
Imidazole Catalysis

Evidence for a Functional Role of the Dynamics of Glycine-121 ofEscherichia coliDihydrofolate Reductase Obtained from Kinetic Analysis of a Site-Directed Mutant†

Biochemistry ◽  
1997 ◽  
Vol 36 (50) ◽  
pp. 15792-15800 ◽  
Author(s):  
Craig E. Cameron ◽  
Stephen J. Benkovic
Keyword(s):  
Kinetic Analysis ◽  
Functional Role ◽  
A Site

scholarly journals pKa Modulation of the Acid/Base Catalyst within GH32 and GH68: A Role in Substrate/Inhibitor Specificity?

PLoS ONE ◽  
2012 ◽  
Vol 7 (5) ◽  
pp. e37453 ◽  
Author(s):  
Shuguang Yuan ◽  
Katrien Le Roy ◽  
Tom Venken ◽  
Willem Lammens ◽  
Wim Van den Ende ◽  
...  
Keyword(s):  
Base Catalyst ◽  
Acid Base ◽  
Inhibitor Specificity ◽  
Substrate Inhibitor

Structure of the epimerization domain of tyrocidine synthetase A

2014 ◽  
Vol 70 (5) ◽  
pp. 1442-1452 ◽  
Author(s):  
Stefan A. Samel ◽  
Paul Czodrowski ◽  
Lars-Oliver Essen
Keyword(s):  
Amino Acids ◽  
Active Site ◽  
Base Catalyst ◽  
Donor Side ◽  
Acid Base ◽  
Bacillus Brevis ◽  
Peptide Synthetases ◽  
Acceptor Side ◽  
Peptide Carrier ◽  
Resolution Structure

Tyrocidine, a macrocyclic decapeptide fromBacillus brevis, is nonribosomally assembled by a set of multimodular peptide synthetases, which condense two D-amino acids and eight L-amino acids to produce this membrane-disturbing antibiotic. D-Phenylalanine, the first amino acid incorporated into tyrocidine, is catalytically derived from enzyme-bound L-Phe by the C-terminal epimerization (E) domain of tyrocidine synthetase A (TycA). The 1.5 Å resolution structure of the cofactor-independent TycA E domain reveals an intimate relationship to the condensation (C) domains of peptide synthetases. In contrast to the latter, the TycA E domain uses an enlarged bridge region to plug the active-site canyon from the acceptor side, whereas at the donor side a latch-like floor loop is suitably extended to accommodate the αIII helix of the preceding peptide-carrier domain. Additionally, E domains exclusively harbour a conserved glutamate residue, Glu882, that is opposite the active-site residue His743. This active-site topology implies Glu882 as a candidate acid–base catalyst, whereas His743 stabilizes in the protonated state a transient enolate intermediate of the L↔D isomerization.

Extreme (109) acidification of adenine-NH2 in an open platinated nucleobase quartet. A pH switch with potential as a biological acid/base catalyst

2001 ◽  
pp. 2058 ◽  
Author(s):  
Marc S. Lüth ◽  
Michael Willermann ◽  
Bernhard Lippert
Keyword(s):  
Base Catalyst ◽  
Acid Base

Reverse Protonation Is the Key to General Acid−Base Catalysis in Enolase†,‡

Biochemistry ◽  
2003 ◽  
Vol 42 (27) ◽  
pp. 8298-8306 ◽  
Author(s):  
Paul A. Sims ◽  
Todd M. Larsen ◽  
Russell R. Poyner ◽  
W. Wallace Cleland ◽  
George H. Reed
Keyword(s):  
Base Catalysis ◽  
Acid Base ◽  
General Acid ◽  
Reverse Protonation
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