Comparison of the Binuclear Metalloenzymes Diphosphoglycerate-Independent Phosphoglycerate Mutase and Alkaline Phosphatase: Their Mechanism of Catalysis via a Phosphoserine Intermediate
Author:
Affiliation:
1. Department of Microbiology, University of Alabama at Birmingham, 933 19th Street South, CHSB-19 Room 545, Birmingham, Alabama 35294, and Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06032
Publisher
American Chemical Society (ACS)
Subject
General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/cr000253a
Reference73 articles.
1. Structure and Mechanism of Alkaline Phosphatase
2. Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus
3. Mechanism of Catalysis of the Cofactor-independent Phosphoglycerate Mutase from Bacillus stearothermophilus
4. Phosphoglycerate mutase from wheat germ: studies with oxygen-18-labeled substrate, investigations of the phosphatase and phosphoryl transfer activities, and evidence for a phosphoryl-enzyme intermediate
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