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Glutamate synthase and the synthesis of glutamate in plants.

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Glutamate synthase and the synthesis of glutamate in plants. / Lea, Peter John; Miflin, Ben J.
In: Plant Physiology and Biochemistry, Vol. 41, No. 6-7, 06.2003, p. 555-564.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Lea, PJ & Miflin, BJ 2003, 'Glutamate synthase and the synthesis of glutamate in plants.', Plant Physiology and Biochemistry, vol. 41, no. 6-7, pp. 555-564. https://doi.org/10.1016/S0981-9428(03)00060-3

APA

Lea, P. J., & Miflin, B. J. (2003). Glutamate synthase and the synthesis of glutamate in plants. Plant Physiology and Biochemistry, 41(6-7), 555-564. https://doi.org/10.1016/S0981-9428(03)00060-3

Vancouver

Lea PJ, Miflin BJ. Glutamate synthase and the synthesis of glutamate in plants. Plant Physiology and Biochemistry. 2003 Jun;41(6-7):555-564. doi: 10.1016/S0981-9428(03)00060-3

Author

Lea, Peter John ; Miflin, Ben J. / Glutamate synthase and the synthesis of glutamate in plants. In: Plant Physiology and Biochemistry. 2003 ; Vol. 41, No. 6-7. pp. 555-564.

Bibtex

@article{e0b39abdf627473489050a35a7751c5c,
title = "Glutamate synthase and the synthesis of glutamate in plants.",
abstract = "The discovery of glutamate synthases (E.C. 1.4.1.13 and E.C. 1.4.7.1) caused a major re-assessment of the way in which ammonium is assimilated in bacteria and higher plants. The history of that discovery is reviewed and considered in the light of recent developments in the biochemistry and genetics of the higher plant ferredoxin- and NADH-dependent enzymes. The evidence is consistent with the view that plants synthesise glutamate from ammonia by the combined activity of glutamine synthetase (E.C. 6.3.1.2) and glutamate synthase (the glutamate synthase cycle) and that glutamate dehydrogenase (GDH, E.C. 1.4.1.2) plays no significant part in glutamate formation. The evidence does, however, suggest an important role for GDH as a catabolic shunt to ensure N metabolism does not adversely affect mitochondrial function and to enable the synthesis of N-rich transport compounds during nitrogen remobilisation.",
keywords = "Ammonia assimilation, Enzyme mechanisms, Gene expression, Glutamate dehydrogenase, Glutamate synthase, Higher plants, Localisation",
author = "Lea, {Peter John} and Miflin, {Ben J.}",
year = "2003",
month = jun,
doi = "10.1016/S0981-9428(03)00060-3",
language = "English",
volume = "41",
pages = "555--564",
journal = "Plant Physiology and Biochemistry",
issn = "0981-9428",
publisher = "Elsevier Masson SAS",
number = "6-7",

}

RIS

TY - JOUR

T1 - Glutamate synthase and the synthesis of glutamate in plants.

AU - Lea, Peter John

AU - Miflin, Ben J.

PY - 2003/6

Y1 - 2003/6

N2 - The discovery of glutamate synthases (E.C. 1.4.1.13 and E.C. 1.4.7.1) caused a major re-assessment of the way in which ammonium is assimilated in bacteria and higher plants. The history of that discovery is reviewed and considered in the light of recent developments in the biochemistry and genetics of the higher plant ferredoxin- and NADH-dependent enzymes. The evidence is consistent with the view that plants synthesise glutamate from ammonia by the combined activity of glutamine synthetase (E.C. 6.3.1.2) and glutamate synthase (the glutamate synthase cycle) and that glutamate dehydrogenase (GDH, E.C. 1.4.1.2) plays no significant part in glutamate formation. The evidence does, however, suggest an important role for GDH as a catabolic shunt to ensure N metabolism does not adversely affect mitochondrial function and to enable the synthesis of N-rich transport compounds during nitrogen remobilisation.

AB - The discovery of glutamate synthases (E.C. 1.4.1.13 and E.C. 1.4.7.1) caused a major re-assessment of the way in which ammonium is assimilated in bacteria and higher plants. The history of that discovery is reviewed and considered in the light of recent developments in the biochemistry and genetics of the higher plant ferredoxin- and NADH-dependent enzymes. The evidence is consistent with the view that plants synthesise glutamate from ammonia by the combined activity of glutamine synthetase (E.C. 6.3.1.2) and glutamate synthase (the glutamate synthase cycle) and that glutamate dehydrogenase (GDH, E.C. 1.4.1.2) plays no significant part in glutamate formation. The evidence does, however, suggest an important role for GDH as a catabolic shunt to ensure N metabolism does not adversely affect mitochondrial function and to enable the synthesis of N-rich transport compounds during nitrogen remobilisation.

KW - Ammonia assimilation

KW - Enzyme mechanisms

KW - Gene expression

KW - Glutamate dehydrogenase

KW - Glutamate synthase

KW - Higher plants

KW - Localisation

U2 - 10.1016/S0981-9428(03)00060-3

DO - 10.1016/S0981-9428(03)00060-3

M3 - Journal article

VL - 41

SP - 555

EP - 564

JO - Plant Physiology and Biochemistry

JF - Plant Physiology and Biochemistry

SN - 0981-9428

IS - 6-7

ER -