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Analysis of Active Site Residues in Escherichia coli Chorismate Mutase by Site-Directed Mutagenesis

✍ Scribed by Liu, David R.; Cload, Sharon T.; Pastor, Richard M.; Schultz, Peter G.


Book ID
126942789
Publisher
American Chemical Society
Year
1996
Tongue
English
Weight
119 KB
Volume
118
Category
Article
ISSN
0002-7863

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Analysis of the active-site residues of a fully functional chorismate mutase representing the N-terminal 113 amino acids of the Escherichia coli P-protein suggests that Lys39 and Gln88 play critical roles in catalyzing the rearrangement of chorismate to prephenate. Five site-directed mutants at thes