Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch. [electronic resource]
Producer: 20071011Description: 24697-706 p. digitalISSN:- 0021-9258
- Adenosine Monophosphate -- chemistry
- Allosteric Site
- Binding Sites
- Dose-Response Relationship, Drug
- Escherichia coli -- enzymology
- Fructose-Bisphosphatase -- antagonists & inhibitors
- Gluconeogenesis
- Glucose-6-Phosphate -- chemistry
- Kinetics
- Models, Biological
- Models, Chemical
- Models, Molecular
- Molecular Conformation
- Stereoisomerism
- Time Factors
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Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
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