Transient kinetics of aminoglycoside phosphotransferase(3′)-IIIa reveals a potential drug target in the antibiotic resistance mechanism
- Biology, ChemistryFEBS letters
Enzyme Inhibition in Open Systems
- BiologyThe Journal of Biological Chemistry
Investigations of the open system behavior of reversible dead-end inhibitors indicated that substrate-competitive inhibition may often be an inappropriate basis for design of potential therapeutic agents, and chemical analogs of pathogen-specific enzymic reaction products rather than analogS of substrates provide a promising basis for the systematic design of such uncompetitive inhibitors.
Solution kinetics measurements suggest HIV-1 protease has two binding sites for darunavir and amprenavir.
- Chemistry, BiologyJournal of medicinal chemistry
Kinetic analysis for wild type and mutant protease showed mixed-type competitive-uncompetitive inhibition for darunavir and the chemically related amprenavir, while saquinavir showed competitive inhibition.
Side chain interactions at the dimer interface of Vibrio alkaline phosphatase determine its reactivity, stability and desthiobiotin inhibition
- Biology, Chemistry
This study assessed a possible inhibition of desthiobiotin (DDB) on VAP, which is used to elute purified enzyme samples of Strep-Tactin® affinity columns and is likely of a mixed noncompetitive nature.
Basic models for differential inhibition of enzymes.
- Biology, ChemistryBiochemical and biophysical research communications
Kinetic Studies for the Inhibition Effect of Pentachlorophenol on Alkaline Phosphatase Activity In Vitro
- Chemistry, Biology
The inhibition kinetic parameters of pentachlorophenol on bovine intestinal mucosa alkaline phosphatase (ALP) activity were studied by spectrophotometry and indicated that the nature of the inhibition was of an uncompetitive type.
Properties Needed for the Enzymes of an Interconvertible Cascade to Generate a Highly Sensitive Response
The understanding of the mechanisms that allow a high degree of sensitivity should constitute a major goal of any theory of metabolic control, as the sensitivity of the pathway to the effector is decreased accordingly.
The Basic Mechanisms of Inhibition and Nonessential Activation
This chapter discusses representative examples that span several branches of the biological sciences and discusses substrates and reaction products in the role of modifiers within the mechanisms to which they belong.
Teaching Enzyme Kinetics and Mechanism in the 21 st Century
The teaching of enzyme kinetics has been neglected in recent years, with the growth in influence of molecular biology, but its importance has not diminished and it has become clear that it has to be combined with stoicheiometric analysis, knowledge of metabolic networks and analysis of enzyme regulation.
Interplay between tetrameric structure, enzymatic activity and allosteric regulation of human dipeptidyl-peptidase I.
- Biology, ChemistryArchives of biochemistry and biophysics
SHOWING 1-10 OF 11 REFERENCES
The effect of natural selection on enzymic catalysis.
- BiologyJournal of molecular biology
Catalysis, binding and enzyme-substrate complementarity
- BiologyProceedings of the Royal Society of London. Series B. Biological Sciences
Two corollaries of this are that intermediates accumulating after the initial Michaelis complex are undesirable and also enzymes whose function is to optimize reaction rates should have evolved to exhibit KM values above those of accessible substrate concentrations.
Limitation of Metabolite Concentrations and the Conservation of Solvent Capacity in the Living Cell
On the mechanism of inhibition of intestinal alkaline phosphatase by L-phenylalanine. I. Kinetic studies.
- Biology, ChemistryThe Journal of biological chemistry
Modern theories of metabolic control and their applications
- BiologyBioscience reports
Existing, qualitative notions with respect to the way in which enzyme properties control metabolism are discussed in the light of the control analysis developed by H. Kacser and J. A. Burns ((1973)…
A Linear Steady-State Treatment of Enzymatic Chains Critique of the Crossover Theorem and a General Procedure to Identify Interaction Sites with an Effector
It is concluded that for real systems the identification of the interaction sites of an effector with an enzymatic chain cannot be achieved by the simple crossover theorem, and even the Identification of “rate controlling” or “regulatory important” enzymes by means of c crossover must be done with great caution.
Quantification of the importance of individual steps in the control of aromatic amino acid metabolism.
- Biology, ChemistryThe Biochemical journal
The quantitative importance of the individual steps of aromatic amino acid metabolism in rat liver was determined by calculation of the respective Control Coefficient (Strengths) by finding that the transport of phenylalanine was responsible for the remaining control in the pathway.
Rate Control of Biological Processes (Davies
- D.D. ed.)