Glutamate Synthetase in Developing Cotyledons of Pisum sativum
- 1 June 1976
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 57 (6), 862-866
- https://doi.org/10.1104/pp.57.6.862
Abstract
Glutamate synthetase (glutamine[amide]:.alpha. ketoglutarate amino transferase oxidoreductase) activity was demonstrated in the developing cotyledons of P. sativum L. cv. ''Burpeeana.'' The enzyme appears to be soluble and is specific for glutamine as amide donor. The enzyme activity is greater with NADH than with NADPH as electron donor. The glutamate synthetase in the developing cotyledon probably provides a mechanism by which the amide N of glutamine, from the translocatory stream, is converted into the amino N of glutamate; transamination reactions involving this synthesized glutamate could provide the amino groups for the biosynthesis of the seed protein amino acids.This publication has 12 references indexed in Scilit:
- Asparagine Metabolism—Key to the Nitrogen Nutrition of Developing Legume SeedsPlant Physiology, 1975
- Glutamine and asparagine as nitrogen donors for reductant-dependent glutamate synthesis in pea rootsBiochemical Journal, 1975
- Induction of glutamate synthase during nodule development in lupinFEBS Letters, 1975
- Alternative route for nitrogen assimilation in higher plantsNature, 1974
- Glutamate synthetase type activity in higher plantsFEBS Letters, 1974
- Specificity for Nicotinamide Adenine Dinucleotide by Nitrate Reductase from LeavesPlant Physiology, 1974
- Evidence for the presence of glutamate synthase in extracts of carrot cells culturesBiochemical and Biophysical Research Communications, 1974
- Protein Synthesis in Cotyledons of Pisum sativum LPlant Physiology, 1972
- Analytical separations by high-voltage paper electrophoresis. Amino acids in protein hydrolysatesBiochemical Journal, 1961
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951