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Furthermore, we find that Swf1 is highly specific for its substrates, as it is unable to substitute for other PATs.
We provide evidence indicating that Swf1 is highly specific for its substrates since it cannot complement pfa3Δ or pfa4Δ strains, even when overexpressed.
The mechanisms that determine the selectivity of MTORC1 for its substrates are not clear, but it has been recently shown that rapamycin, a natural inhibitor of MTORC1, reduces the phosphorylation of EIF4EBP1and RPS6 with different sensitivity.
Thereby, mRNA binding sites in TS overlap with the binding sites for its substrates, methylenetetrahydrofolate and dUMP and therefore, mRNA and substrate are in direct competition.
This increase in fluorescence is perhaps due to a compaction of the hydrophobic core which leads to an increase in the affinity for its substrates.
Since we assayed the enzyme using coupled assays which could be prone to errors that could account for the high affinity of the mycobacterial enzyme for its substrates and the higher catalytic efficiency, compared to its other prokaryotic counterparts, we chose to quantify the kinetic parameters also using a direct, thermodynamic approach (Table 1).
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For example glucokinase (Glk1p, EC 2.7.1.2) has lower activity than the two hexokinases (Hxk1p and Hxk2p, EC 2.7.1.1); however it also has a higher affinity for its substrate glucose (see Table 2), allowing it to operate effectively at low substrate concentrations.
Furthermore, lower Km for substrate indicated that it had high affinity for its substrate and lower value of Vmax indicated that a small amount of enzyme can convert substrate into the product.
It is actually uncharacterized functionally for its substrate in H. pylori.
In addition, the K m value of the immobilized SMDH was lower than the free SMDH, and it indicated that immobilized SMDH had an apparently higher affinity for its substrate than that of the free enzyme.
MurD ligase is highly stereospecific for its substrate, d-glutamic acid (d-Glu).
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