Interactions and spatial arrangement of spin-labeled NAD+ bound to glyceraldehyde-3-phosphate dehydrogenase. Comparison of EPR and X-ray modeling data.-Reference-Cited by-同舟云学术

Interactions and spatial arrangement of spin-labeled NAD+ bound to glyceraldehyde-3-phosphate dehydrogenase. Comparison of EPR and X-ray modeling data.

Published:1984-08 Issue:15 Volume:259 Page:9717-9728
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Beth A H,Robinson B H,Cobb C E,Dalton L R,Trommer W E,Birktoft J J,Park J H

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

1. Negative cooperativity in enzyme action. Binding of diphosphopyridine nucleotide to glyceraldehyde-3-phosphate dehydrogenase

2. The Properties and Enzymatic Significance of the Enzyme-Diphosphopyridine Nucleotide Compound of 3-Phosphoglyceraldehyde Dehydrogenase

3. The role of the nicotinamide moiety of NAD+ for negative cooperativity in glyceraldehyde-3-phosphate dehydrogenase as studied by spin-labeled cofactors

4. Glyceraldehyde 3-phosphate dehydrogenases

5. Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase

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