The role of arginine residues in the function of d-glyceraldehyde-3-phosphate dehydrogenase
- 1 January 1978
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Enzymology
- Vol. 527 (2), 319-326
- https://doi.org/10.1016/0005-2744(78)90346-7
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- Structural studies on glyceraldehyde-phosphate dehydrogenase from rat skeletal muscleBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Arginyl Residues: Anion Recognition Sites in EnzymesScience, 1977
- A study of the ionic properties of the essential histidine residue of yeast alcohol dehydrogenase in complexes of the enzyme with its coenzymes and substratesBiochemical Journal, 1977
- Anion binding sites in the active center of d-glyceraldehyde-3-phosphate dehydrogenaseJournal of Molecular Biology, 1976
- Specificity of induced conformational changes. Case of yeast glyceraldehyde-3-phosphate dehydrogenaseBiochemistry, 1975
- Essential arginine residues in d-glyceraldehyde-3-phosphate dehydrogenaseBiochimica et Biophysica Acta (BBA) - Protein Structure, 1975
- Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenaseJournal of Molecular Biology, 1974
- Use of a thermal inactivation technique to obtain binding constants for the Escherichia coli valyl-tRNA synthetaseArchives of Biochemistry and Biophysics, 1972
- Inhibition and kinetic mechanism of rabbit muscle glyceraldehyde-3-phosphate dehydrogenaseBiochemistry, 1972
- The isolation and specific activity of rabbit-muscle glyceraldehyde phosphate dehydrogenaseBiochemical Journal, 1964