Effect of Substrate Inhibition and Cooperativity on the Electrochemical Responses of Glucose Dehydrogenase. Kinetic Characterization of Wild and Mutant Types

2011 ◽  
Vol 133 (32) ◽  
pp. 12801-12809 ◽  
Author(s):  
Fabien Durand ◽  
Benoît Limoges ◽  
Nicolas Mano ◽  
François Mavré ◽  
Rebeca Miranda-Castro ◽  
...  
Keyword(s):  
Glucose Dehydrogenase ◽  
Substrate Inhibition ◽  
Kinetic Characterization

scholarly journals Kinetic characterization of a cocaine hydrolase engineered from mouse butyrylcholinesterase

2015 ◽  
Vol 466 (2) ◽  
pp. 243-251 ◽  
Author(s):  
Xiabin Chen ◽  
Xiaoqin Huang ◽  
Liyi Geng ◽  
Liu Xue ◽  
Shurong Hou ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Inhibition ◽  
Kinetic Characterization ◽  
Substrate Activation ◽  
Amino Acid Mutations ◽  
Human Butyrylcholinesterase

Mouse (mBChE) and human butyrylcholinesterase (hBChE)-based cocaine hydrolases (mCocH and hCocH) have remarkably different catalytic efficiencies against cocaine, but with little differences in catalytic efficiencies against acetylcholine (ACh) and butyrylthiocholine (BTC). The amino-acid mutations have remarkably converted substrate activation of the enzymes into substrate inhibition.

In Vitro Reconstitution and Kinetic Characterization of the Essential Condensation Enzymes Involved in Prodiginine and Tambjamine Biosynthesis

2019 ◽  
Author(s):  
Katherine J. Picott ◽  
Julie A. Deichert ◽  
Ella M. deKemp ◽  
Avena Ross
Keyword(s):  
Substrate Inhibition ◽  
Kinetic Characterization ◽  
Reaction Sequence ◽  
Ping Pong ◽  
In Vitro Reconstitution

We have reconstituted<i> </i>the <i>in vitro</i> activity of the purified condensation enzymes PigC and TamQ, from prodiginine and tambjamine pathways respectively. Upon analysis and comparison of their kinetic profiles, a ping-pong reaction sequence with substrate inhibition was identified for each condensation enzyme.

In Vitro Reconstitution and Kinetic Characterization of the Essential Condensation Enzymes Involved in Prodiginine and Tambjamine Biosynthesis

2019 ◽  
Author(s):  
Katherine J. Picott ◽  
Julie A. Deichert ◽  
Ella M. deKemp ◽  
Avena Ross
Keyword(s):  
Substrate Inhibition ◽  
Kinetic Characterization ◽  
Reaction Sequence ◽  
Ping Pong ◽  
In Vitro Reconstitution

We have reconstituted<i> </i>the <i>in vitro</i> activity of the purified condensation enzymes PigC and TamQ, from prodiginine and tambjamine pathways respectively. Upon analysis and comparison of their kinetic profiles, a ping-pong reaction sequence with substrate inhibition was identified for each condensation enzyme.

Kinetic Characterization of Anticarsia gemmatalis Digestive Serine- Proteases and the Inhibitory Effect of Synthetic Peptides

2018 ◽  
Vol 24 (11) ◽  
Author(s):  
Adriana M. Patarroyo-Vargas ◽  
Yaremis B. Merino-Cabrera ◽  
Jose C. Zanuncio ◽  
Francelina Rocha ◽  
Wellington G. Campos ◽  
...  
Keyword(s):  
Synthetic Peptides ◽  
Serine Proteases ◽  
Inhibitory Effect ◽  
Anticarsia Gemmatalis ◽  
Kinetic Characterization

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases

Kinetic characterization of a slow-binding inhibitor of Bla2: thiomaltol

2012 ◽  
Vol 28 (1) ◽  
pp. 137-142 ◽  
Author(s):  
Sara R. Schlesinger ◽  
Britain Bruner ◽  
Patrick J. Farmer ◽  
Sung-Kun Kim
Keyword(s):  
Kinetic Characterization ◽  
Slow Binding Inhibitor
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