Product inhibition kinetics determinations - Substrate interaction affinity and enzymatic kinetics using one quantitative FRET assay

2021 ◽  
Author(s):  
Yan Liu ◽  
Fan Zhang ◽  
Ling Jiang ◽  
J. Jefferson P. Perry ◽  
Zhihe Zhao ◽  
...  
Keyword(s):  
Product Inhibition ◽  
Inhibition Kinetics ◽  
Substrate Interaction ◽  
Enzymatic Kinetics

Concomitant substrate and product inhibition kinetics in lactic acid production

1991 ◽  
Vol 13 (4) ◽  
pp. 314-319 ◽  
Author(s):  
L.M.D. Gonçalves ◽  
A.M.R.B. Xavier ◽  
J.S. Almeida ◽  
M.J.T. Carrondo
Keyword(s):  
Lactic Acid ◽  
Acid Production ◽  
Lactic Acid Production ◽  
Product Inhibition ◽  
Inhibition Kinetics

Substrate and product inhibition kinetics in succinic acid production by Actinobacillus succinogenes

2008 ◽  
Vol 41 (2) ◽  
pp. 128-135 ◽  
Author(s):  
Sze Ki Carol Lin ◽  
Chenyu Du ◽  
Apostolis Koutinas ◽  
Ruohang Wang ◽  
Colin Webb
Keyword(s):  
Succinic Acid ◽  
Acid Production ◽  
Product Inhibition ◽  
Actinobacillus Succinogenes ◽  
Inhibition Kinetics ◽  
Succinic Acid Production

scholarly journals A product-inhibition study of the mechanism of mitochondrial octanoyl-coenzyme A synthetase

1969 ◽  
Vol 111 (3) ◽  
pp. 257-262 ◽  
Author(s):  
A. B. Graham ◽  
M. V. Park
Keyword(s):  
Coenzyme A ◽  
Liver Mitochondria ◽  
Product Inhibition ◽  
Inhibition Kinetics ◽  
Inhibition Study ◽  
Ping Pong ◽  
Kinetics Of ◽  
Allosteric Activator

By a study of the product-inhibition kinetics of the octanoyl-CoA synthetase from ox liver mitochondria, evidence was obtained consistent with the hypothesis that the enzyme reacts by a Bi Uni Uni Bi Ping Pong type of mechanism in which the order of addition and evolution of substrates and products is CoA, octanoate, octanoyl-CoA, ATP, PPi and AMP. There is also evidence that more than one molecule of CoA can add to the enzyme and that it may act as an allosteric activator.

scholarly journals Purification and kinetics of phenylpropanoid O-methyltransferase activities from Brassica oleracea

1989 ◽  
Vol 67 (11-12) ◽  
pp. 763-769 ◽  
Author(s):  
Emidio De Carolis ◽  
Ragai K. Ibrahim
Keyword(s):  
Competitive Inhibition ◽  
Divalent Cations ◽  
Product Inhibition ◽  
Affinity Column ◽  
Ph Optimum ◽  
Substrate Interaction ◽  
Interaction Kinetics ◽  
Molecular Masses ◽  
Inhibition Studies ◽  
Kinetics Of

Two phenylpropanoid O-methyltransferase isoforms were purified to homogeneity from young cabbage leaves. They catalyzed the meta-O-methylation of caffeic and 5-hydroxyferulic acids to ferulic and sinapic acids, respectively. Both isoforms I and II exhibited different elution patterns from a Mono Q column, distinct apparent pIs on chromatofocusing, different product ratios, and stability on adenosine–agarose affinity column. On the other hand, both isoforms had similar apparent molecular masses (42 kilodaltons) and a pH optimum of 7.6. They exhibited no requirement for divalent cations and were both irreversibly inhibited by iodoacetate. Substrate interaction kinetics of the more stable isoform I, using the 5-hydroxyferulic acid and S-adenosyl-L-methionine, gave converging lines. Product inhibition studies showed competitive inhibition between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine and non-competitive inhibition between the phenylpropanoid substrate and its methylated product. The kinetic patterns are consistent with an ordered bi bi mechanism, where S-adenosyl-L-methionine is the first substrate to bind and S-adenosyl-L-homocysteine is the last product released.Key words: phenylpropanoid O-methyltransferase, purification, isoforms, adenosine–agarose affinity chromatography, kinectic mechanism.

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