Sentence examples for reduction in km from inspiring English sources

This reduction in KM enables improved selectivity in complex cell lysates systems, as the concentration used in assays is directly related to the KM.

The reduction in Km ranged from 3 to 6.5-fold, with the highest reduction in Km observed with the K9me3 and K9ac effector peptides, in addition to the unmodified H3 10mer peptide.

The reduction in Km for the peptide substrate alone suggests that effector peptide binding to the PHD1 domain allosterically promotes binding of peptide substrates in KDM5A.

This approximate fivefold reduction in Km is also observed when the Ac-H3K4me2 21mer peptide is used as a substrate (Fig. 2c, Table 2).

One of the reasons for the reduction in Km could be an increase in the affinity of the enzyme for ATP.

This only partially agrees with the findings of Takahashi et al.[4] who showed no significant difference in Vmax but did show a reduction in Km for the V38A variant, suggesting this substitution results in stronger binding of the DHT substrate (Table 1).

The D113A/N substitutions resulted in reductions in Km and kcat values, which paralleled the reductions in KiATP and Ki' ATP values.

Although a reduction in the Km for D-glucose was achieved, the Km was still an order of magnitude better than for D-xylose, while the Vmax for D-glucose uptake even increased up to twofold.

For Mn2+-dependent nucleotide insertion, most of the variants (including the Δ1 25 variant) showed the kcat/ Km values similar to those of wild-type, whereas the R96G variant displayed 29- to 41-fold reduction in kcat/ Km compared to wild-type (Table 5).

Together, our investigations of the impact of H3 modifications on PHD1 binding and KDM5A catalysis indicate a similar reduction in the Km of demethylation when PHD1 is saturated with effector peptide (Fig. 4b).

However, the reduction in the Km value for xylotetraose (X4) results in a greater catalytic efficiency towards this substrate.