scholarly journals Transition State Analogues of Enzymatic Reaction as Potential Drugs

10.5772/52504 ◽  
2013 ◽  
Author(s):  
Karolina Gluza ◽  
Pawel Kafarski
Keyword(s):  
Transition State ◽  
Enzymatic Reaction ◽  
Transition State Analogues

scholarly journals New human renin inhibitory peptides. Angiotensinogen transition-state analogues containing novel Leu-Val replacement and a retro-inverso amide bond.

1988 ◽  
Vol 36 (6) ◽  
pp. 2278-2281 ◽  
Author(s):  
Kinji Iizuka ◽  
Tetsuhide Kamijo ◽  
Hiromu Harada ◽  
Kenji Akahane ◽  
Tetsuhiro Kubota ◽  
...  
Keyword(s):  
Transition State ◽  
Amide Bond ◽  
Inhibitory Peptides ◽  
Transition State Analogues ◽  
Human Renin

scholarly journals Tight Binding of Transition-State Analogues to a Peptidyl-Aminoacyl-L/D-Isomerase from Frog Skin

ChemBioChem ◽  
2011 ◽  
Vol 12 (13) ◽  
pp. 1996-2000 ◽  
Author(s):  
Verena Gehmayr ◽  
Christa Mollay ◽  
Lorenz Reith ◽  
Norbert Müller ◽  
Alexander Jilek
Keyword(s):  
Transition State ◽  
Frog Skin ◽  
Tight Binding ◽  
Transition State Analogues

scholarly journals Polyvalent transition-state analogues of sialyl substrates strongly inhibit bacterial sialidases.

2020 ◽  
Author(s):  
coralie assailly ◽  
clarisse bridot ◽  
amélie saumonneau ◽  
paul lottin ◽  
Benoit Roubinet ◽  
...  
Keyword(s):  
Transition State ◽  
Important Class ◽  
Inhibitory Potency ◽  
Polymeric Scaffolds ◽  
Transition State Analogues

<div>Conjugation of the transitionstate-cation analogue DANA to polymeric scaffolds led to highly potent inhibitors of bacterial sialidases. Each clustered DANA on the polymers saw its inhibitory potency for S. pneumoniae or B. thetaiotaomicron sialidases improved by more than four orders of magnitude. This extends the multivalent concept to this important class of enzymes.</div><div><br></div>

scholarly journals Arg-158 Is Critical in Both Binding the Substrate and Stabilizing the Transition-state Oxyanion for the Enzymatic Reaction of Malonamidase E2

2006 ◽  
Vol 281 (52) ◽  
pp. 40057-40064 ◽  
Author(s):  
Young Sung Yun ◽  
Wook Lee ◽  
Sejeong Shin ◽  
Byung-Ha Oh ◽  
Kwan Yong Choi
Keyword(s):  
Transition State ◽  
Enzymatic Reaction

Phosphotransfer and Nucleotidyltransfer

2007 ◽  
Author(s):  
Perry A. Frey ◽  
Adrian D. Hegeman
Keyword(s):  
Transition State ◽  
Molecular Mechanisms ◽  
Enzymatic Reaction ◽  
Covalent Bond ◽  
Phosphoryl Group ◽  
Dissociative Mechanism ◽  
Chemical Mechanisms ◽  
Cellular Processes ◽  
Nucleic Acid Biosynthesis ◽  
Transfer Mechanisms

Phosphotransferases, phosphatases, and nucleotidyltransferases catalyze nucleophilic substitution at phosphorus. They constitute a dominant class of enzymes in intermediary metabolism, energy transduction, nucleic acid biosynthesis and processing, and regulation of many cellular processes, including replication, cellular development, and apoptosis. The mechanisms of the action of these enzymes have been studied intensively at several levels, ranging from the biosynthesis of metabolites and nucleic acids to unmasking signaling networks to elucidating the molecular mechanisms of catalysis. We focus on the chemical mechanisms of the reactions of biological phosphates. More than 40 years of research on this chemistry reveals that the mechanisms can be grouped into two classes: the phosphoryl group (PO3−) transfer mechanisms and the nucleotidyl or alkylphosphoryl group (ROPO2−) transfer mechanisms. Because the fundamental chemical mechanisms of these reactions are not treated in textbooks, we begin by considering this chemistry and then move on to the enzymatic reaction mechanisms. Phosphomonoesters, phosphoanhydrides, and phosphoramidates undergo substitution at phosphorus by transfer of the phosphoryl (PO3–) group, that is, by P—O and P—N cleavage. The current description of a typical phosphoryl group transfer mechanism is one in which the phosphoryl donor and acceptor interact weakly with the phosphoryl group in flight in a transition state in which the total bonding to phosphorus is decreased relative to the ground state. The bonding is weak between phosphorus and the leaving group R–X and between phosphorus and the accepting group Y in the transition state of. Because of decreased bonding to phosphorus, this is a loose transition state that has been described as dissociative. The latter should not be confused with the dissociative mechanism, which is considered later. To avoid confusion, we use the term loose transition state. Detailed studies indicate that the bonding denoted by the dashed lines in represents partial covalency on the order of 10% to 20% of the strength of a full covalent bond, or a bond order of 0.1 to 0.2.

scholarly journals Transition-State Analogues of Phenylethanolamine N-Methyltransferase

2020 ◽  
Vol 142 (33) ◽  
pp. 14222-14233 ◽  
Author(s):  
Niusha Mahmoodi ◽  
Rajesh K. Harijan ◽  
Vern L. Schramm
Keyword(s):  
Transition State ◽  
Transition State Analogues

scholarly journals Crystal Structures ofStaphylococcus aureusKetol-Acid Reductoisomerase in Complex with Two Transition State Analogues that Have Biocidal Activity

2017 ◽  
Vol 23 (72) ◽  
pp. 18289-18295 ◽  
Author(s):  
Khushboo M. Patel ◽  
David Teran ◽  
Shan Zheng ◽  
Ajit Kandale ◽  
Mario Garcia ◽  
...  
Keyword(s):  
Transition State ◽  
Crystal Structures ◽  
Biocidal Activity ◽  
Transition State Analogues
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