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Unfortunately, broader substrate specificity of some glycosidases can be taken into account by assigning of more EC numbers to one enzyme only.
This may underpin the broader substrate specificity of the heterodimeric transporters although the substrate-binding sites of ABCDs remain to be identified.
In addition, the SPM-1 active site is notably wider than those of the B2 MBLs (Fig. S3 †), possibly contributing to the broader substrate specificity of SPM-1 (which hydrolyzes all β-lactams except monobactams) compared to the B2 MBLs (which are narrow-spectrum carbapenemases).
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A possible explanation for a low number of reactions is the use of a single generic reaction to model the broad substrate specificity of an enzyme instead of explicitly describing each specific reaction separately with the same EC number.
The transgenic plants also showed moderate tolerance and accumulation of arsenic (As) upon exogenous As stress, signifying broad substrate specificity of OsMTP1.
Substrate specificity of two homoisocitrate dehydrogenases derived from Deinococcus radiodurans and Saccharomyces cerevisiae was analyzed using a series of synthetic substrate analogs, which indicated a relatively broad substrate specificity of these enzymes.
Analysis of the structure explains the broad substrate specificity of the enzyme, and provides the basis for rational design of novel prodrugs and for site-directed mutagenesis for improved enzyme activity.
These structures formed the basis for molecular dynamics simulations to understand the broad substrate specificity of this enzyme and the role of active site residues in the phospho-transfer mechanism and oligomerization.
Comparison of the PDZ1 LPA2 structure to the structure of PDZ1 in complex with a different peptide provides insights into the diverse nature of PDZ1 substrate recognition and suggests that the conformational flexibility in the ligand binding pocket is involved in determining the broad substrate specificity of PDZ1.
This hypothesis may be supported by the broad substrate specificity of KDPG aldolase identified biochemically [28] and structurally [29].
Fad enzymes, including the broad substrate specificity of the FACS, have also been characterized in Pseudomonas fragi [31] [33].
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