Results 341 to 350 of about 2,040,864 (360)

Molting fluid chitinase: A homotropic allosteric enzyme

Biochemical and Biophysical Research Communications, 1979
Abstract The molting fluid of the tobacco hornworm has chitinase activity which shows allosteric behavior with chitin. A parabolic curve is obtained on a double reciprocal plot of 1 v vs. 1 [S] , and a sigmoid curve results when v (N-acetylglucosamine produced) is plotted against [S] (chitin concentration in terms of N-acetylglucosamine ...
Maria L. Bade, Alfred Stinson
openaire   +3 more sources

Kinetic Analysis of Allosteric Enzymes

1971
Publisher Summary Allosteric enzymes are defined as those enzymes that can mediate indirect interactions between distinct sites. They are characterized by a sigmoidal response of the initial rate to increasing substrate or inhibitor concentration. An increasing number of allosteric enzymes exhibit another type of deviation of the binding curves for ...
openaire   +2 more sources

Active site directed effectors of allosteric enzymes

Biochimica et Biophysica Acta (BBA) - Enzymology, 1975
This communication introduces the concept of an active site directed effector, in terms of the two state model of Monod et al. (Monod, J., Wyman, J. and Changeux, J.-P. (1965) J. Mol. Biol. 12, 88-118), a consideration made necessary by the observation that the activity of a number of enzymes of the control type is modulated by effector molecules whose
P.W. Kuchel, Geoffrey D. Smith, D.V. Roberts   +2 more
openaire   +3 more sources

Dissociation of Enzyme Oligomers: A Mechanism for Allosteric Regulation

Critical Reviews in Biochemistry and Molecular Biology, 1994
Most enzymes exist as oligomers or polymers, and a significant subset of these (perhaps 15% of all enzymes) can reversibly dissociate and reassociate in response to an effector ligand. Such a change in subunit assembly usually is accompanied by a change in enzyme activity, providing a mechanism for regulation.
openaire   +3 more sources

Cooperative effects in hemoglobin and allosteric enzymes

1970 IEEE Symposium on Adaptive Processes (9th) Decision and Control, 1970
Cooperative effects in the binding of oxygen to hemoglobin have been known and studied for some time. The degree of cooperativity is reflected in the S or sigmoid saturation curve (i.e. percentage of oxygenated hemoglobin as a function of the partial pressure of oxygen) showing that the binding of a few oxygen molecules favours the binding of more and ...
openaire   +2 more sources

Allosteric Enzyme- and Transporter-Based Interactions

2009
Allosterism in enzymes and transporters can result in alterations in kinetic profiles and in rates of metabolism and transport. Cooperativity due to allosteric interactions has been observed with drug-metabolizing enzymes such as the cytochromes P450 and the uridine glucuronosyltransferases.
Timothy S. Tracy, Murali Subramanian
openaire   +2 more sources

Selective Covalent Inhibition of “Allosteric Cys121” Distort the Binding of PTP1B Enzyme: A Novel Therapeutic Approach for Cancer Treatment

Cell Biochemistry and Biophysics, 2019
Shama Khan, Imane Bjij, M. Soliman
semanticscholar   +1 more source

Visualizing allosteric pathways in oligomeric enzymes

2023
Visualizing molecular structures and their interactions is essential for understanding their function. A number of computer programs that serve this purpose have become indispensable tools in this niche. Programs such as Pymol, Chimera, and Coot, to mention perhaps the most known examples, all have their devoted followers based on their strengths and ...
openaire   +1 more source

Allosteric regulation of enzyme activity.

Advances in enzymology and related areas of molecular biology, 1966
openaire   +3 more sources

Allosteric Enzymes

2004
openaire   +1 more source