Role of Lysine-183 in d-Glyceraldehyde-3-Phosphate Dehydrogenases. Properties of the N-Acetylated Yeast, Sturgeon Muscle and Rabbit Muscle Enzymes
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1978.tb12074.x/fullpdf
Reference57 articles.
1. Subunit structure of glyceraldehyde-3-phosphate dehydrogenase
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5. Binding and properties of NAD+ in glyceraldehydephosphate dehydrogenase from lobster-tail muscle
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1. Structural, Kinetic and Proteomic Characterization of Acetyl Phosphate-Dependent Bacterial Protein Acetylation;PLoS ONE;2014-04-22
2. Étude comparative de la modification chimique des groupes sulfhydryles des glycéraldéhyde-3-phosphate déshydrogénases de levure et de muscle de lapin;Biochimie;1982-07
3. Structure and Reactive Relationship in Glyeeraledehyde-3-Phosphate Dehydrogenase. Dinitrophenylation of Cysteine Residues of Yeast and Rabbit Muscle Enzymes;European Journal of Biochemistry;1981-10
4. Structural and functional consequences of subunit interactions in glyceraldehyde 3-phosphate dehydrogenase;Biochimie;1981-02
5. Structure of lobster apo-d-glyceraldehyde-3-phosphate dehydrogenase at 3.0 Å resolution;Journal of Molecular Biology;1980-04
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