Crystallographic Studies of the Catalytic and a Second Site in Fumarase C from Escherichia coli,
Author:
Affiliation:
1. Department of Biochemistry, University of Minnesota, Minneapolis, Minnesota 55455
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi9614702
Reference37 articles.
1. Studies of the Enzyme Fumarase. III.1 The Dependence of the Kinetic Constants at 25° upon the Concentration and pH of Phosphate Buffers
2. The modification with tetranitromethane of an essential tyrosine in the active site of pig fumarase
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