An Electron Transport System in Maize Roots for Reactions of Glutamate Synthase and Nitrite Reductase

Suzuki, Akira; Oaks, Ann; Jacquot, Jean‐Pierre; Vidal, Jean; Gadal, Pierre

doi:10.1104/pp.78.2.374

Cited by 81 publications

(22 citation statements)

References 22 publications

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“…The Fd-dependent GOGATs range in mol wt from 125 to 180 kD, are usually localized in chloroplasts, and are involved in the assimilation of NH3 derived from the light dependent reduction of NO3 and from photorespiration (20,29). The Fd-GOGAT form has also been demonstrated in roots (20)(21)(22) and most recently in soybean (Glycine max L. Merr) nodules (23). The NAD(P)H-dependent GOGATs have been reported in roots (20), shoots (12,22,24), and nodules (2,9) and ranged in mol wt from 200 to 240 kD.…”

mentioning

confidence: 98%

“…These values agree quite closely with those found for lupine nodule GOGAT (1). Low cofactor Kms have been demonstrated in Fd-GOGATs from soybean nodules and rice leaves (Kms 1.3-7.0 ,uM) (20)(21)(22)(23).…”

Section: Enzyme Characteristicsmentioning

confidence: 99%

“…The NAD(P)H-dependent GOGATs have been reported in roots (20), shoots (12,22,24), and nodules (2,9) and ranged in mol wt from 200 to 240 kD. Antibodies have been produced to rice (Oryza sativa L.) (22) and maize (Zea mays L.) (21) leaf Fd-GOGAT. Monocot root Fd-GOGAT is antigenically quite different than the leaf enzyme, suggesting that they are distinct proteins (20)(21)(22)(23).…”

mentioning

confidence: 99%

“…Antibodies have been produced to rice (Oryza sativa L.) (22) and maize (Zea mays L.) (21) leaf Fd-GOGAT. Monocot root Fd-GOGAT is antigenically quite different than the leaf enzyme, suggesting that they are distinct proteins (20)(21)(22)(23). Antibodies to Fd-GOGAT generally do not recognize NAD(P)H-GOGATs, thus suggesting that these enzymes are also structurally distinct proteins.…”

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confidence: 99%

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Purification and Characterization of NADH-Glutamate Synthase from Alfalfa Root Nodules

Anderson¹,

Vance²,

Heichel³

et al. 1989

Plant Physiol.

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Glutamate synthase (GOGAT), a key enzyme in the pathway for the assimilation of symbiotically fixed dinitrogen (N2) into amino acids in alfalfa (Medicago sativa L.) root nodules, was purified and used to produce high titer polyclonal antibodies. Purification resulted in a 208-fold increase in specific activity to 13 micromole per minute per milligram of protein and an activity yield of 37%. Further purification to near homogeneity was achieved by fast protein liquid chromatography, but with substantial loss of activity. Enzymic activity was highly labile, losing 3% per hour even when substrates, stabilizers, and reducing agents were included in buffers. However, activity could be partially stabilized for up to 1 month by storing GOGAT at -800C in 50% glycerol. The subunit molecular weight of GOGAT was estimated at 200 ± 7 kilodaltons with a native molecular weight of 235 ± 16 kilodaltons, which suggested that GOGAT is a monomer of unusually high molecular weight. The pi was estimated to be 6.6. The Km values for glutamine, a-ketoglutarate, and NADH were 466, 33, and 4.2 micromolar, respectively. Antibodies were produced to NADH-GOGAT. Specificity of the antibodies was shown by immunotitration of GOGAT activity. Alfalfa nodule NADH-GO-GAT antibodies cross-reacted with polypeptides of a similar molecular weight in a number of legume species. Westem blots probed with anti-GOGAT showed that the high GOGAT activity of nodules as compared to roots was associated with increased levels of GOGAT polypeptides. Nodule NADH-GOGAT appeared to be highly expressed in effective nodules and little if any in other organs.

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confidence: 98%

Section: Enzyme Characteristicsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Purification and Characterization of NADH-Glutamate Synthase from Alfalfa Root Nodules

Anderson¹,

Vance²,

Heichel³

et al. 1989

Plant Physiol.

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“…which is antigenically similar to spinach-leaf Fd-N ADP reductase and transfers electrons from NADPH or NADJI to spinach-leaf Fd. has been characterized in young maize roots (SUZUKI et al 1985).…”

mentioning

confidence: 99%

Nitrite reduction system in barley roots: existence of an electron carrier operating in an electron-transport sequence from glucose-6-phosphate to nitrite reductase

Oji

Komatsu

Taguchi³

et al. 1989

Soil Science and Plant Nutrition

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Ferredoxin and Ferredoxin-Dependent Enzymes

Knaff

1996

Oxygenic Photosynthesis: The Light Reactions

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An Electron Transport System in Maize Roots for Reactions of Glutamate Synthase and Nitrite Reductase

Cited by 81 publications

References 22 publications

Purification and Characterization of NADH-Glutamate Synthase from Alfalfa Root Nodules

Purification and Characterization of NADH-Glutamate Synthase from Alfalfa Root Nodules

Nitrite reduction system in barley roots: existence of an electron carrier operating in an electron-transport sequence from glucose-6-phosphate to nitrite reductase

Ferredoxin and Ferredoxin-Dependent Enzymes

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