Chemical modification of the functional arginine residue(s) of malic enzyme from Zea mays
- 2 January 1991
- journal article
- Published by Elsevier in Phytochemistry
- Vol. 30 (2) , 431-435
- https://doi.org/10.1016/0031-9422(91)83699-l
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Kinetic and Structural Properties of NADP-Malic Enzyme from Sugarcane LeavesPlant Physiology, 1990
- Essential Arginyl Residues in the Plasma Membrane H+-ATPase from Vigna radiata L. (Mung Bean) RootsPlant Physiology, 1988
- Presence of essential histidine residues in nadp-malic enzyme from maizePhytochemistry, 1987
- Precautions when determining kinetically the order of inactivation of enzymes by functionally irreversible inhibitorsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Modification of essential arginine residues of pigeon liver malic enzymeBiochimica et Biophysica Acta (BBA) - Enzymology, 1981
- Origin of the Selectivity of α‐Dicarbonyl Reagents for Arginyl Residues of Anion‐Binding SitesEuropean Journal of Biochemistry, 1980
- Equilibrium substrate binding studies of the malic enzyme of pigeon liver. Equivalence of nucleotide sites and anticooperativity associated with the binding of L-malate to the enzyme-manganese(II)-reduced nicotinamide adenine dinucleotide phosphate ternary complexBiochemistry, 1980
- NADP-malic enzyme from maize leaf: Purification and propertiesArchives of Biochemistry and Biophysics, 1979
- Functional arginyl residues in carboxypeptidase A. Modification with butanedioneBiochemistry, 1973
- Active site modification of isocitrate lyaseBiochemical and Biophysical Research Communications, 1969