scholarly journals Noncompetitive Inhibition of Indolethylamine-N-methyltransferase by N,N-Dimethyltryptamine and N,N-Dimethylaminopropyltryptamine

Biochemistry ◽  
2014 ◽  
Vol 53 (18) ◽  
pp. 2956-2965 ◽  
Author(s):  
Uyen B. Chu ◽  
Sevahn K. Vorperian ◽  
Kenneth Satyshur ◽  
Kelsey Eickstaedt ◽  
Nicholas V. Cozzi ◽  
...  
Keyword(s):  
Noncompetitive Inhibition

Differential Pharmacologies of Mecamylamine Enantiomers: Positive Allosteric Modulation and Noncompetitive Inhibition

2008 ◽  
Vol 328 (2) ◽  
pp. 525-532 ◽  
Author(s):  
Nikolai B. Fedorov ◽  
Lisa C. Benson ◽  
John Graef ◽  
Patrick M. Lippiello ◽  
Merouane Bencherif
Keyword(s):  
Allosteric Modulation ◽  
Noncompetitive Inhibition

scholarly journals Mechanism for Noncompetitive Inhibition by Novel GluN2C/D N-Methyl-d-aspartate Receptor Subunit-Selective Modulators

2011 ◽  
Vol 80 (5) ◽  
pp. 782-795 ◽  
Author(s):  
Timothy M. Acker ◽  
Hongjie Yuan ◽  
Kasper B. Hansen ◽  
Katie M. Vance ◽  
Kevin K. Ogden ◽  
...  
Keyword(s):  
Receptor Subunit ◽  
Noncompetitive Inhibition ◽  
Aspartate Receptor

scholarly journals Structural Bases of Noncompetitive Inhibition of AMPA-Subtype Ionotropic Glutamate Receptors by Antiepileptic Drugs

Neuron ◽  
2016 ◽  
Vol 91 (6) ◽  
pp. 1305-1315 ◽  
Author(s):  
Maria V. Yelshanskaya ◽  
Appu K. Singh ◽  
Jared M. Sampson ◽  
Chamali Narangoda ◽  
Maria Kurnikova ◽  
...  
Keyword(s):  
Glutamate Receptors ◽  
Antiepileptic Drugs ◽  
Ionotropic Glutamate Receptors ◽  
Noncompetitive Inhibition

Noncompetitive Inhibition of Hepatocyte Growth Factor-dependent Met Signaling by a Phage-derived Peptide

2009 ◽  
Vol 385 (1) ◽  
pp. 79-90 ◽  
Author(s):  
Eric M. Tam ◽  
Steven T. Runyon ◽  
Lydia Santell ◽  
Clifford Quan ◽  
Xiaoyi Yao ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Noncompetitive Inhibition ◽  
Hepatocyte Growth

Noncompetitive inhibition by aluminum, scandium and yttrium of acetylcholinesterase from Electrophorus electricus

1982 ◽  
Vol 31 (7) ◽  
pp. 1437-1440 ◽  
Author(s):  
Judith K. Marquis ◽  
Andrew J. Lerrick
Keyword(s):  
Noncompetitive Inhibition ◽  
Electrophorus Electricus

Some properties of phosphodiesterase I from microsomes of rat intestinal mucosa

1970 ◽  
Vol 48 (10) ◽  
pp. 1151-1159 ◽  
Author(s):  
I. Hynie ◽  
S. H. Zbarsky
Keyword(s):  
Intestinal Mucosa ◽  
Assay System ◽  
Noncompetitive Inhibition ◽  
Optimum Ph ◽  
Nitrophenyl Ester

Some properties of phosphodiesterase I from microsomes of rat intestinal mucosa were studied using the p-nitrophenyl ester of thymidine 5′-phosphate as substrate. The optimum pH was found to be 9.5–9.6 in several buffer systems. The activity was destroyed at temperatures of 63–68°, depending on the pH of the medium. Mg2+, Ca2+, Sr2+, Ba2+, and Ni2+ had a variable activating effect while Al3+, Cu2+, and Be were inhibitory. The enzyme was inhibited completely by 10−5 M EDTA or EGTA in the assay system used. The evidence obtained suggested phosphodiesterase I is a metal-requiring enzyme. Glycine, bicine, and tricine inhibited the enzyme at higher concentrations. Cysteine, 2-mercaptoethanol, and dithiothreitol were strongly inhibitory at a concentration of 10−3 M. The Km of the enzyme was 8.5 × 10−4 M. In 6 M urea 40% of the activity of the enzyme was lost irreversibly after 24 h at 4°. In 3 M urea there was an immediate and reversible mixed competitive–noncompetitive inhibition and the Km was increased seven to eight times.

MECHANISM OF ACTION OF THE LACTIC DEHYDROGENASE OF THE MAMMALIAN ERYTHROCYTE: I. INFLUENCE OF INHIBITORS

1958 ◽  
Vol 36 (10) ◽  
pp. 1075-1083 ◽  
Author(s):  
Paul Ottolenghi ◽  
Orville F. Denstedt
Keyword(s):  
Mechanism Of Action ◽  
Lactic Dehydrogenase ◽  
Noncompetitive Inhibition ◽  
Mammalian Erythrocyte ◽  
Lactate And Pyruvate

This paper pertains to the inhibition of lactic dehydrogenase by substances structurally related to its substrates, pyruvate and lactate. Oxalate, tartronate, and malonate inhibit the enzyme in a competitive manner towards lactate, and in a noncompetitive manner towards pyruvate. Phenoxyacetate causes simultaneous competitive and noncompetitive inhibition towards both lactate and pyruvate. The results obtained lead to the conclusion that, for their activation, pyruvate and lactate react with different sites on the enzyme surface.

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