Search PubMed⌕ Search

PubMed · 7341250

The specific velocity plot. A graphical method for determining inhibition parameters for both linear and hyperbolic enzyme inhibitors.

Abstract

A new method is described for plotting kinetic results for inhibited enzymatic reactions. The plot is particularly designed for the analysis of hyperbolic, mixed-type inhibitors, but can be applied to any other linear system. The method consists of plotting experimental data in a normalized way, as v0/vi versus the specific velocity sigma/(1 + sigma), where v0/vi represents the ratio of the initial velocities for the non-inhibited and inhibited reactions at a given substrate concentration [S], and sigma is the [S]/Km ratio. The procedure provides a simple way of determining the inhibition constants Ki and Ki', i.e, the dissociation constants of the EI and ESI complexes, respectively, and the velocity saturation values.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

A Baici. 1981. The specific velocity plot. A graphical method for determining inhibition parameters for both linear and hyperbolic enzyme inhibitors.. https://doi.org/10.1111/j.1432-1033.1981.tb05570.x

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Slow-binding inhibition of soybean lipoxygenase-1 by dodecyl gallate.

Dodecyl gallate inhibited the soybean lipoxygenase-1 (EC 1.13.11.12, type-1) catalyzed peroxidation of linoleic acid with an IC50 of 0.007 microM without being oxidized. The progress curves for enzyme reactions were recorded by both spectrophotometric and polarographic methods, and the inhibition kinetics revealed competitive and slow-binding inhibition. Both the initial velocity and steady-state rate in the progress curve decreased with increasing dodecyl gallate. The kinetic parameters that described the inhibition by dodecyl gallate were evaluated by nonlinear regression fits.

Enzyme Inhibitors↗

Modeling zinc enzyme inhibition with functional thiolate ligands.

The blocking of zinc enzymes by thiolate-containing inhibitors was modeled by treating TpPh,MeZn-OH with functional thiols. The latter were chosen such that they contain an additional donor function (COOH, COOR, NH2, NHR, OH) in a position favorable for chelation. Of them, mercapto carboxylic acid esters were incorporated as thiolates. The corresponding mercapto carboxylic acids, however, used only their carboxylate function for coordination. Various mercapto amines, mercapto alcohols, and mercaptophenol were exclusively converted to thiolate ligands. The two modes of inhibitor attachment, terminal or chelating, were observed equally frequently. As a rule, they occur as alternatives for similar ligands. In case of 2-mercaptophenol they coexist in the crystalline state and in solution. Hydrogen bonding, both intra- and intermolecular, seems to be a decisive factor determining the inhibitor attachments. Its persistence in solution is underlined by the observation that TpPh,MeZn-hydroxythiophenolates are methylated about 2 orders of magnitude slower than TpPh,MeZn-SPh itself.

Enzyme Inhibitors↗