Attapulgite-supported magnetic dual acid-base catalyst for the catalytic conversion of lignin to phenolic monomers

2019 ◽  
Vol 94 (4) ◽  
pp. 1269-1281 ◽  
Author(s):  
Zhen Wu ◽  
Jun Zhang ◽  
Xinxu Zhao ◽  
Xun Li ◽  
Yu Zhang ◽  
...  
Keyword(s):  
Catalytic Conversion ◽  
Base Catalyst ◽  
Acid Base

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

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.

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