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Insights into the Mechanism of Escherichia coli Methionine Aminopeptidase from the Structural Analysis of Reaction Products and Phosphorus-Based Transition-State Analogues †,‡

✍ Scribed by Lowther, W. Todd; Zhang, Yan; Sampson, Peter B.; Honek, John F.; Matthews, Brian W.


Book ID
125484767
Publisher
American Chemical Society
Year
1999
Tongue
English
Weight
569 KB
Volume
38
Category
Article
ISSN
0006-2960

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A high-resolution structure of Escherichia coli aspartate transcarbamoylase has been determined to 2.1 Å; resolution in the presence of the bisubstrate analog N-phosphonacetyl-L-aspartate (PALA). The structure was refined to a free R-factor of 23.4% and a working R-factor of 20.3%. The PALA molecule