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The synthetases (LeuRS and TrpRS) activating the remaining analogs in the lower right quadrant of the graph (A19, A21 23 and C9) have especially low Kms (1.5 µM [59] and 12 µM [60] respectively) for their cognate AAs.
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The advantage of this enzyme over the PDI from all other sources is its low KM.
This model suggests that the most effective inhibitors are those with very low apparent Vmax and very low Km values.
These results indicate that, although rat CYP1B1 is a low Km E2 hydroxylase, its product ratio, unlike the human enzyme, favors 2-hydroxylation.
And a low Km value, 0.6 mM, was observed, indicating a good affinity of functional ligand on the nanocapsule towards methyl parathion.
Double mutant 93R94H showed comparable high rates and low Km values for NADPH (kcat 20 s−1, Km 6 μM) and NADH (kcat 25 s−1, Km 9 μM) with retention of 70%% of wild type activity towards NADH.
Compared with bioactive horseradish peroxidase (HRP), the synthesized ISPtNP exhibited a low Km value (~0.12 mM) and a high Kcat value (~2.27 × 104 s−1) for 3,3′,5,5′-tetramethylbenzidine 3,3′,5,5′-tetramethylbenzidineiliTMBand pH tolerance.
The increased understanding of hASNase3 function resulting from these studies reveals the key regions that govern cleavage and the asparaginase reaction, which may inform the design of variants that attain a low KM for asparagine.
Enzymes with the double changes at 225 and 274 (mutant G225A-A274F) showed, apart the substantial low Km value for NADPH and its high catalytic efficiency, kinetic parameters relative to coenzymes which were not additive over the single substitutions.
But, for N-benzoyl tyrosyl para nitrophenyl ester, the mimic exhibited low kcat as well as low Km values, consistent with the nonproductive binding exhibited by natural chymotrypsin for hydrophobic substrate.
The canonical SET domain shared by most KMTs has low Km for SAM [15].
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