Suggestions(4)
Exact(26)
Apparent Km values were increased in whole cell incubations with luciferin H suggesting impaired access of the substrate to the active site of the enzymes in whole cells.
Replacement of another conserved residue Ala/Gly by a Phe sterically blocks the access of the substrate to the active site.
Overall, in view of the results, we propose that the presence of non-structured amino acid in the N-terminal leads to destabilization of the xylanases and may promote less access of the substrate to the active site.
Based on the model structure of the enzyme and substrate docking simulation, we predicted the key residues that appear to enhance the access of the substrate to the active site of the enzyme, and constructed numerous OPH mutants.
Higher substrate concentrations may have created steric hindrance in the access of the substrate to the enzyme active site due to diffusion limitations of the substrate into the gel matrix.
In addition, the nature of the support and its polarity can also affect the enzyme conformation, as well as the partition of substrates and products from the enzyme environment, which might prevent the access of the substrate to the enzyme active site.
Similar(34)
Interestingly, TPH2B presented the highest Vmax, which was twice as high as for TPH2A and well in accordance with the prediction that the GK insertion into the hinge region allows easier access of the substrates to the catalytic core.
A request for virtual network establishment consists of a list of access nodes of the substrate, as well as of a traffic matrix that represents the amount of traffic transferred between the access nodes listed.
In our model, these residues are located at the access channel of the substrate F420 (near the loop 164GKGK mentioned above) and may be involved in substrate binding.
A semi-open climate chamber is designed for convenient access of the sample substrate, while maintaining the climate around the droplet on the sample.
For example, the DNA methyltransferase, Dnmt 1, preferentially methylates hemimethylated CpG sites on DNA after DNA replication, and Bashtrykov et al. report that the ubiquitin-like PHD and RING finger domains protein 1 (Uhrf1) allosterically activates Dnmt 1 by unblocking an inhibitory domain of Dnmt 1, thus allowing better access of the CpG substrate to the active site of Dnmt 1.
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