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通过谷氨酰胺合成酶和谷氨酸合酶在景天酸代谢植物四角葡萄中进行氨固定

Ammonia Fixation via Glutamine Synthetase and Glutamate Synthase in the CAM Plant Cissus quadrangularis L.

作者信息

Berger M G, Sprengart M L, Kusnan M, Fock H P

机构信息

Universität Kaiserslautern, Fachbereich Biologie, Postfach 3049, 6750 Kaiserslautern, Federal Republic of Germany.

出版信息

Plant Physiol. 1986 Jun;81(2):356-60. doi: 10.1104/pp.81.2.356.

DOI:10.1104/pp.81.2.356
PMID:16664820
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1075339/
Abstract

Succulent stems of Cissus quadrangularis L. (Vitaceae) contain glutamine synthetase, glutamate synthase, and glutamate dehydrogenase. The CO(2) and water gas exchanges of detached internodes were typical for Crassulacean acid metabolism plants. During three physiological phases, e.g. in the dark, in the early illumination period after stomata closure, and during the late light phase with the stomata wide open, (15)NH(4)Cl was injected into the central pith of stem sections. The kinetics of (15)N labeling in glutamate and glutamine suggested that glutamine synthetase was involved in the initial ammonia fixation. In the presence of methionine sulfoximine, an inhibitor of glutamine synthetase, the incorporation of (15)N derived from (15)NH(4)Cl was almost completely inhibited. Injections of amido-(15)N glutamine demonstrated a potential for (15)N transfer from the amido group of glutamine into glutamate which was suppressed by the glutamate synthase inhibitor, azaserine. The evidence indicates that glutamine synthetase and glutamate synthase could assimilate ammonia and cycle nitrogen during all phases of Crassulacean acid metabolism.

摘要

四角叶白粉藤(葡萄科)的肉质茎含有谷氨酰胺合成酶、谷氨酸合酶和谷氨酸脱氢酶。离体节间的二氧化碳和水汽交换是景天酸代谢植物的典型特征。在三个生理阶段,即在黑暗中、气孔关闭后的早期光照期以及气孔完全开放的后期光照阶段,将(15)氯化铵注入茎段的中央髓部。谷氨酸和谷氨酰胺中(15)N标记的动力学表明谷氨酰胺合成酶参与了最初的氨固定。在谷氨酰胺合成酶抑制剂甲硫氨酸亚砜亚胺存在的情况下,源自(15)氯化铵的(15)N掺入几乎被完全抑制。酰胺-(15)N谷氨酰胺的注射表明存在谷氨酰胺酰胺基团中的(15)N向谷氨酸转移的潜力,而这种转移被谷氨酸合酶抑制剂重氮丝氨酸所抑制。证据表明,谷氨酰胺合成酶和谷氨酸合酶可在景天酸代谢的所有阶段同化氨并循环氮。

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Ammonia Fixation via Glutamine Synthetase and Glutamate Synthase in the CAM Plant Cissus quadrangularis L.通过谷氨酰胺合成酶和谷氨酸合酶在景天酸代谢植物四角葡萄中进行氨固定
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本文引用的文献

1
An electron transport system in maize roots for reactions of glutamate synthase and nitrite reductase : physiological and immunochemical properties of the electron carrier and pyridine nucleotide reductase.玉米根中谷氨酸合酶和亚硝酸盐还原酶反应的电子传递系统:电子载体和吡啶核苷酸还原酶的生理和免疫化学性质。
Plant Physiol. 1985 Jun;78(2):374-8. doi: 10.1104/pp.78.2.374.
2
Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots.从玉米苗线粒体中制备的谷氨酸脱氢酶的特性。
Plant Physiol. 1984 Dec;76(4):1009-13. doi: 10.1104/pp.76.4.1009.
3
Glutamic Acid metabolism and the photorespiratory nitrogen cycle in wheat leaves: metabolic consequences of elevated ammonia concentrations and of blocking ammonia assimilation.小麦叶片中的谷氨酸代谢与光呼吸氮循环:氨浓度升高及氨同化受阻的代谢后果
Plant Physiol. 1984 May;75(1):60-6. doi: 10.1104/pp.75.1.60.
4
Glutamine Synthetases of Higher Plants : Evidence for a Specific Isoform Content Related to Their Possible Physiological Role and Their Compartmentation within the Leaf.高等植物的谷氨酰胺合成酶:与它们可能的生理作用及其在叶片中的区室化相关的特定同工型含量的证据。
Plant Physiol. 1983 May;72(1):22-5. doi: 10.1104/pp.72.1.22.
5
Variable Photosynthetic Metabolism in Leaves and Stems of Cissus quadrangularis L.叶片和茎中叶片光合作用代谢的变化
Plant Physiol. 1983 Mar;71(3):677-9. doi: 10.1104/pp.71.3.677.
6
Rhythms in glutamine synthetase activity, energy charge, and glutamine in sunflower roots.向日葵根系中谷氨酰胺合成酶活性、能量电荷和谷氨酰胺的节律。
Plant Physiol. 1982 Dec;70(6):1683-8. doi: 10.1104/pp.70.6.1683.
7
Evidence for the Glutamine Synthetase/Glutamate Synthase Pathway during the Photorespiratory Nitrogen Cycle in Spinach Leaves.菠菜叶片光呼吸氮循环过程中谷氨酰胺合成酶/谷氨酸合酶途径的证据
Plant Physiol. 1982 Nov;70(5):1514-7. doi: 10.1104/pp.70.5.1514.
8
Nitrate Assimilation and Crassulacean Acid Metabolism in Leaves of Kalanchoë fedtschenkoi Variety Marginata.金边虎尾兰叶片硝酸盐同化和景天科酸代谢。
Plant Physiol. 1981 Aug;68(2):464-8. doi: 10.1104/pp.68.2.464.
9
Regulatory effects of ammonia on carbon metabolism in photosynthesizing Chlorella pyrenoidosa.氨对光合小球藻碳代谢的调控作用。
Biochim Biophys Acta. 1970 Jun 30;205(3):401-8. doi: 10.1016/0005-2728(70)90106-4.