Sentence examples for binding of one substrate from inspiring English sources

If two substrates bind to the same active site on the same enzyme so that binding of one substrate prevents the binding of the other, then the two substrates are said to be "competitive" inhibitors.

(1198) The sites exhibited positive cooperativity, i.e., binding of one substrate stimulated the efflux of the other substrate, and the efflux was maximal when both sites were modified.

As noted above, global fitting of the initial velocity data for the forward reaction catalysed by GmATPS1 did not distinguish between the two possible sequential mechanisms and the interaction factor obtained for a random mechanism suggested that binding of one substrate decreases affinity for the second.

Modelling of the initial velocity data to a random sequential mechanism yields a correlation coefficient (r=0.989) slightly better than the fit to an ordered mechanism (r=0.980), but the interaction factor for the random mechanism was 9.53, which suggests that binding of one substrate is a negative interaction that decreases the affinity for the second substrate.

On the other hand, if substrate binding follows a random mechanism, binding of one substrate to the enzyme would not be a prerequisite for binding of the other, and all four reactions of Scheme 1 can take place with equal probability.

This means that the binding of one substrate molecule affects the binding of subsequent substrate molecules.

Similar modulation of the binding affinity of one substrate by another during sequential binding was previously observed for Pgp [ 35, 48, 50].

It has been shown that binding of one of these substrates (ferredoxin or NADP+) weakens the binding of the other.

These aspects are both in agreement with experimental current measurements, indicating that substrate binding allows the binding of one of the Na+ ions.

Each active site is composed of one PLP binding site, made up mainly of the N-terminal domain of one monomer, and one substrate binding site, made up mainly of the C-terminal domain of the second monomer.

The binding of substrate to one SecYEG appears to induce an inaccessible state in the other, possibly accounting for the preference of the dimer to bind only one copy of the preprotein.