Adenosine di-, tri- and tetraphosphopyridoxals modify the same lysyl residue at the ATP-binding site in adenylate kinase
- 14 March 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 229 (2), 261-264
- https://doi.org/10.1016/0014-5793(88)81137-2
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- NMR studies of the AMP-binding site and mechanism of adenylate kinaseBiochemistry, 1987
- Modification of lactate dehydrogenase by pyridoxal phosphate and adenosine polyphosphopyridoxal.Biochemistry, 1986
- ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins.Proceedings of the National Academy of Sciences, 1986
- NMR studies of the magnesium-ATP binding site of adenylate kinase and of a 45-residue peptide fragment of the enzymeBiochemistry, 1985
- Studies on adenosine triphosphate transphosphorylases. Amino acid sequence of rabbit muscle ATP-AMP transphosphorylaseBiochemistry, 1984
- Substrate positions and induced-fit in crystalline adenylate kinaseJournal of Molecular Biology, 1977
- Amino acid sequence of two functional sites in yeast glycogen phosphorylaseBiochemistry, 1975
- Three-dimensional structure of adenyl kinaseNature, 1974
- The mode of binding of pyridoxal 5′-phosphate in glycogen phosphorylaseBiochemical and Biophysical Research Communications, 1970
- THE REACTION OF SODIUM BOROHYDRIDE WITH MUSCLE PHOSPHORYLASE1Journal of the American Chemical Society, 1958