Kinetics of Allosteric Inhibition of Single Enzyme by Product Molecules

2020 ◽  
Vol 124 (52) ◽  
pp. 11793-11801
Author(s):  
Prasanta Kundu ◽  
Soma Saha ◽  
Gautam Gangopadhyay
Keyword(s):  
Allosteric Inhibition ◽  
Kinetics Of ◽  
Single Enzyme

Titelbild: Single-Enzyme Kinetics of CALB-Catalyzed Hydrolysis (Angew. Chem. 4/2005)

2005 ◽  
Vol 117 (4) ◽  
pp. 499-499
Author(s):  
Kelly Velonia ◽  
Ophir Flomenbom ◽  
Davey Loos ◽  
Sadahiro Masuo ◽  
Mircea Cotlet ◽  
...  
Keyword(s):  
Enzyme Kinetics ◽  
Kinetics Of ◽  
Single Enzyme

scholarly journals Studies of the acetylcholinesterase from houseflies (Musca domestica L.) resistant and susceptible to organophosphorus insecticides

1975 ◽  
Vol 149 (2) ◽  
pp. 463-469 ◽  
Author(s):  
A L Devonshire
Keyword(s):  
Musca Domestica ◽  
Rate Constants ◽  
Gel Electrophoresis ◽  
Organophosphorus Compounds ◽  
Organophosphorus Insecticides ◽  
Triton X ◽  
Kinetics Of ◽  
Kinetics Of Inhibition ◽  
Single Enzyme

Acetylcholinesterase from the heads of insecticide-resistant and -susceptible houseflies (Musca domestica L.) was studied in vitro. The enzymes could not be distinguished electrophoretically, and their behaviour on polyacrylamide-disc-gel electrophoresis was influenced by the presence of Triton X-100 in both the homogenate and the gels. In the absence of detergent, the acetylcholinesterase was heterogeneous, but behaved as a single enzyme when it was present. By analogy with studies of acetylcholinesterase from other sources, these observations were attributed to aggregation of the enzyme when not bound by membranes. The enzyme from resistant flies was more slowly inhibited than the susceptible enzyme, bimolecular rate constants (ki) differing by approx. 4-20-fold for a range of organophosphorus compounds. The kinetics of inhibition of acetylcholinesterase were consistent with the results of electrophoresis, i.e. they corresponded to those of a single enzyme in the presence of Triton X-100, but a mixture of enzymes in its absence. The susceptibility of the more sensitive components in these mixtures was determined.

Single Lipid Vesicle Assay for Characterizing Single-Enzyme Kinetics of Phospholipid Hydrolysis in a Complex Biological Fluid

2013 ◽  
Vol 135 (38) ◽  
pp. 14151-14158 ◽  
Author(s):  
Seyed R. Tabaei ◽  
Michael Rabe ◽  
Henrik Zetterberg ◽  
Vladimir P. Zhdanov ◽  
Fredrik Höök
Keyword(s):  
Enzyme Kinetics ◽  
Biological Fluid ◽  
Lipid Vesicle ◽  
Phospholipid Hydrolysis ◽  
Kinetics Of ◽  
Single Enzyme

Single enzyme electroanalysis

The Analyst ◽  
2021 ◽  
Author(s):  
Kathryn J. Vannoy ◽  
Andrey Ryabykh ◽  
Andrei I. Chapoval ◽  
Jeffrey E. Dick
Keyword(s):  
Experimental Approach ◽  
Electrochemical Methods ◽  
Kinetics Of ◽  
Enzyme Reactivity ◽  
Single Enzyme

Traditional enzymology relies on the kinetics of millions of enzymes, an experimental approach that may wash out heterogeneities between individual enzymes. Electrochemical methods have emerged in the last 5 years to probe single enzyme reactivity.

Sign in / Sign up

Export Citation Format

Share Document