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© 1977 Oxford University Press

RESEARCH-ARTICLE

Studies on Glutamate Synthase from the Leaves of Higher Plants

R. M. WALLSGROVE, E. HAREL 1, P. J. LEA and B. J. MIFLIN

Biochemistry Department, Rothamsted Experimental Station Harpenden, Hertfordshire AL5 2JQ, U.K.

Ferredoxin-dependent glutamate synthase has been isolated and purified 170-fold from field bean (Vicia faba cv. Minor) leaves. The enzyme has a molecular weight of 145 000 and does not appear to contain non-haem iron. The Km values of the enzyme for glutamine, 2-oxoglutarate, and ferredoxin are 330, 150, and 2 µM respectively. The specificity of the enzyme is extremely high and no substitutes for glutamine have been found. Azaserine is a potent inhibitor of glutamate synthase.

Chloroplasts from four species of plants have been shown to carry out a light-dependent glutamate synthesis from glutamine. This reaction is also highly specific for glutamine and purified asparagine cannot substitute for glutamine.


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