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Molecular basis for the herbicide resistance of Roundup Ready crops
The CP4 enzyme has unexpected kinetic and structural properties that render it unique among the known EPSP synthases, and can be restored through a single-site mutation in the active site (Ala-100–Gly), allowing glyphosate to bind in its extended, inhibitory conformation.
Biochemical, Serological, and Virulence Characterization of Clinical and Oyster Vibrio parahaemolyticus Isolates
Concerns are raised about the reliability of the tdh, trh, and T3SS genes as virulence markers and the need for more-detailed pathogenicity investigations of V. parahaemolyticus is highlighted.
The Lipase Engineering Database: a navigation and analysis tool for protein families
The LED has been applied to systematically analyze sequence-structure-function relationships of this vast and diverse enzyme class and is a useful tool to identify functionally relevant residues apart from the active site residues, and to design mutants with desired substrate specificity.
Zinc plays a key role in human and bacterial GTP cyclohydrolase I.
The crystal structure of recombinant human GTP cyclohydrolase I was solved by Patterson search methods by using the coordinates of the Escherichia coli enzyme as a model to contain an essential zinc ion coordinated to a His side chain.
Lipase Engineering Database
More diverse plant communities have higher functioning over time due to turnover in complementary dominant species
More diverse communities have been shown to have higher and more temporally stable ecosystem functioning than less diverse ones, suggesting they should also have a consistently higher level of
Molecular modeling of family GH16 glycoside hydrolases: Potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the poaceae
Family GH16 glycoside hydrolases can be assigned to five subgroups according to their substrate specificities, including xyloglucan transglucosylases/hydrolases (XTHs), (1,3)‐β‐galactanases,
Biosynthesis of vitamin b2 (riboflavin).
The biosynthesis of one riboflavin molecule requires one molecule of GTP and two molecules of ribulose 5-phosphate as substrates and the structure of the biosynthetic enzyme, 6,7-dimethyl-8-ribityllumazine synthase, has been studied in considerable detail.