Pigeon liver malic enzyme: Involvement of an arginyl residue at the binding site for malate and its analogs
- 1 August 1983
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 225 (1) , 296-305
- https://doi.org/10.1016/0003-9861(83)90033-4
Abstract
No abstract availableThis publication has 40 references indexed in Scilit:
- Presence of an essential arginyl residue in D-β-hydroxybutyrate dehydrogenase from mitochondrial inner membraneBiochemical and Biophysical Research Communications, 1980
- 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
- Inhibition and alternate-substrate studies on the mechanism of malic enzymeBiochemistry, 1977
- Essential arginine residues in glutamate dehydrogenaseFEBS Letters, 1976
- Role of arginyl residues in directing carboxymethylation of horse liver alcohol dehydrogenaseBiochemistry, 1975
- Functional arginyl residues as NADH binding sites of alcohol dehydrogenasesBiochemistry, 1974
- Selective chemical modification of arginine residues in mitochondrial malate dehydrogenaseBiochemical and Biophysical Research Communications, 1974
- Protein Structure and Enzymatic Activity, VIII. Participation of Arginyl Residues in the Catalytic Function of Glucose-6-phosphate Dehydrogenase fromCandida utilisHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1970
- A Synthesis for β-Aroylacrylic Acids Substituted with Electron-withdrawing GroupsJournal of the American Chemical Society, 1954