Evidence for an interprotomerial active site in D-glyceraldehyde-3-phosphate dehydrogenase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(75)80929-X/fullpdf
Reference29 articles.
1. Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle
2. Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase
3. Dinitrophenylation and thiolysis in the reversible labeling of a cysteine residue associated with the nicotinamide adenine dinucleotide site of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
4. Reversible dinitrophenylation of glyceraldehyde 3-phosphate dehydrogenase. Identification of the labeled site
5. Introduction of an intramolecular crosslink at the active site of glyceraldehyde 3-phosphate dehydrogenase
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1. Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase.;Proceedings of the National Academy of Sciences;1992-10-15
2. Structural Interactions with Enzymes;The Pyridine Nucleotide Coenzymes;1982
3. Structure of lobster apo-d-glyceraldehyde-3-phosphate dehydrogenase at 3.0 Å resolution;Journal of Molecular Biology;1980-04
4. Role of Lysine-183 in d-Glyceraldehyde-3-Phosphate Dehydrogenases. Properties of the N-Acetylated Yeast, Sturgeon Muscle and Rabbit Muscle Enzymes;European Journal of Biochemistry;1978-02
5. Thiolysis of O-2,4-dinitrophenyltyrosines;Archives of Biochemistry and Biophysics;1977-01
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