Enzymes of Nitrogen Metabolism in Legume Nodules
- 1 October 1977
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 79 (2), 355-362
- https://doi.org/10.1111/j.1432-1033.1977.tb11816.x
Abstract
An NADH-dependent glutamate synthase has been purified 500-fold from the plant cytoplasm fraction of Lupinus angustifolius nodules. It consists of a single polypeptide chain, Mr 235000. The optimum pH is 8.5, at which Km values for 2-oxoglutarate, glutamine and NADH are 39 micrometer, 400 micrometer and 1.3 micrometer respectively. The catalytic centre activity is of the order of 70 s-1 and is independent of pH between 6.5 and 9.5. Glutamate synthase is inhibited by glutamic acid, oxaloacetic acid, aspartic acid and asparagine, all competitive with 2-oxoglutarate; and by NAD+, which is competitive with NADH. There is evidence of two flavine prosthetic groups per enzyme molecule.Keywords
This publication has 10 references indexed in Scilit:
- Ammonia assimilation in lupin nodulesNature, 1976
- The pathway of nitrogen assimilation in plantsPhytochemistry, 1976
- Induction of glutamate synthase during nodule development in lupinFEBS Letters, 1975
- Glutamate Synthase from Escherichia coliPublished by Elsevier ,1972
- [1] Measurement of molecular weights by electrophoresis on SDS-acrylamide gelMethods in Enzymology, 1972
- Molecular weight determinations and the influence of gel density, protein charges and protein shape in polyacrylamide gel electrophoresisJournal of Chromatography A, 1970
- 1 Steady State KineticsPublished by Elsevier ,1970
- 1 X-Ray Crystallography and Enzyme StructurePublished by Elsevier ,1970
- The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel ElectrophoresisJournal of Biological Chemistry, 1969
- Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresisArchives of Biochemistry and Biophysics, 1968