Die Glucose-6-phosphat Dehydrogenase im Stoffwechsel photoautotropher Organismen

Eichhorn, M.; Corbus, B.

doi:10.1016/s0015-3796(88)80001-5

Cited by 11 publications

(7 citation statements)

References 114 publications

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“…The optimal pH values and the apparent Km values from spruce roots are in good agreement with published values for photoautotrophic organisms in general (G6PDH: Eichhorn and Corbus 1988;6PGDH: Adkins et al 1980;ICADH: Chen and Gadal 1990). Our data (Table 2) from vegetative tissue of spruce compare favourably with data from gametophytes of Larix laricina (Table 4;Pitel and Cheliak 1986).…”

Section: Discussionsupporting

confidence: 88%

“…Whether this phenomenon stems from positive cooperativity in binding to the respective substrate or from the existence of multiple forms of the enzymes in the crude extracts must await further analyses employing purified enzymes. The strict substrate specificity with respect to NADP is common for G6PDH (Eichhorn and Corbus 1988) and ICADH (the NAD dependent activity usually represents only approximately 2% of the NADP-linked enzyme, Chen and Gadal 1990) from plant tissues.…”

Section: Discussionmentioning

confidence: 99%

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Kinetic and electrophoretic characterization of NADP dependent dehydrogenases from root tissues of Norway spruce [Picea abies (L.) Karst.] employing a rapid one-step extraction procedure

Guttenberger

Schaeffer

Hampp

1994

Trees

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Summary. The NADPH generating enzymes glucose-6-phosphate dehydrogenase (EC 1.1.1.49), 6-phosphogluconate dehydrogenase (EC 1.1.1.44), and isocitrate-dehydrogenase (NADP dependent; EC 1.1.1.42) have been characterized in spruce [Picea abies (L.) Karst.] roots. Interference from inherent phenolic compounds was minimized by complexation with borate and insoluble polyvinylpyrrolidone in the presence of 2-mercaptoethanol and NADP. A further addition of protective substances had no (bovine serum albumin) or even an inhibitory effect (ascorbate) on the enzyme activities. The enzymes were shown to be strictly NADP specific. The optimal pH values and the apparent Michaelis constants from spruce roots are in good agreement with data from different photosynthetic organisms and gametophytic tissues of conifers. Native electrophoresis and subsequent activity staining showed the same banding patterns for enzymes both from root and needle tissues. In addition, the applicability of a highly sensitive dot-blot assay for the accurate quantification of the extracted protein is shown.

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Section: Discussionsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Kinetic and electrophoretic characterization of NADP dependent dehydrogenases from root tissues of Norway spruce [Picea abies (L.) Karst.] employing a rapid one-step extraction procedure

Guttenberger

Schaeffer

Hampp

1994

Trees

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“…The results of kinetic studies are shown in Table 2; the puriˆed G6PDH1 of Chlorella has structural and kinetic properties comparable with those reported Downloaded by [Umeå University Library] at 14:17 09 October 2014 from other sources 38,39) including a potato cytosolic enzyme. 9) For example, Chlorella G6PDH1 has similar parameters to cytosolic G6PDH from potato (Km values of 260 mM for G6P and 6 mM for NADP).…”

Section: Properties Of the Puriˆed G6pdh Isoformssupporting

confidence: 61%

Purification and Characterization of Two Isoforms of Glucose 6-Phosphate Dehydrogenase (G6PDH) fromChlorella vulgarisC-27

Honjoh¹,

Mimura²,

Kuroiwa³

et al. 2003

Bioscience, Biotechnology, and Biochemistry

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Two kinds of isoforms of glucose 6-phosphate dehydrogenase (G6PDH) were purified from cells of a freezing-tolerant strain, Chlorella vulgaris C-27, by sequential steps of chromatography on five kinds of columns, including a HiTrap Blue column which showed excellent separation of the isoforms from each other. The two isoforms (G6PDH1 and G6PDH2) were purified up to 109-fold and 197-fold with specific activity of 14.4 and 26.0 U/mg-protein, respectively. G6PDH1 showed an apparent Mr of 200,000 with a subunit Mr of about 58,000, whereas G6PDH2 showed an apparent Mr of 450,000 with a subunit Mr of about 52,000. The kinetic parameters were measured and several enzymatic features of the isoforms, such as effects of metal ions on the enzyme activity, were clarified, which showed that the two isoforms were different from each other in many respects. Among the effective ions, Cd2+ showed marked stimulating effects on both isoforms. G6PDH1 and G6PDH2 seem to be a cytosolic and a chloroplastic type, respectively, as judged by their sensitivity to DTT, and also from the results of sequence similarity searches using their N-terminal and internal amino acid sequences.

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“…Glucose-6-phosphate dehydrogenase (G6P DH; D-glucose-6-phosphate: NADP + oxidoreductase, EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (6PG DH; 6-phospho-D-gluconate: NADP + oxidoreductase, EC 1.1.1.44) play an important role in the regulation of the flux through the pathway at the level of its first enzyme G6P DH, which in conjunction with 6-phosphogluconolactonase, which hydrolyses 6-phospho-D-gluconate lactone to 6-phospho-D-gluconate, form an efficient irreversible enzyme system (Turner and Turner 1980). G6P DH is present in plant tissues in the form of two main isozyme complexes, one of which is located in the chloroplasts and the other in the cytosol (Eichhorn and Corbus 1988). Both isozymes show similar properties (nearly the same pH optima, relative molecular mass, kinetic constants K m and V max , etc.…”

Section: Introductionmentioning

confidence: 99%

Correlation of viral RNA biosynthesis with glucose-6-phosphate dehydrogenase activity and host resistance

Šindelář

Šindelářová

2002

Planta

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Changes in glucose-6-phosphate dehydrogenase (G6P DH; EC 1.1.1.49) activity caused by infection of tobacco ( Nicotiana tabacum L.) leaves with potato virus Y (PVY), cucumber mosaic virus, potato virus X, tobacco rattle virus and turnip mosaic virus, the subcellular localisation of G6P DH isozymes in mesophyll protoplasts derived from healthy and PVY-infected tobacco leaves, as well as G6P DH control and the relationship of its isozymes with the degree of tobacco resistance to PVY multiplication, were studied. The activities of G6P DH were markedly increased in locally and systemically infected leaves and the time courses of the activity linearly correlated with those of virus multiplication. In leaves infected with PVY, the activity time courses of the crude and the partially purified G6P DH were coincident. This probably indicates the involvement of coarse regulation of the enzyme. PVY content linearly correlated with enhanced G6P DH activity in leaf discs derived from susceptible, tolerant and resistant cultivars of tobacco. The increased activity of the enzyme in infected protoplasts and plant tissues was predominantly caused by the increased activity of chloroplastic isozymes. This was confirmed by the specific staining of isozymes after electrophoretic separation of chloroplastic proteins of tobacco leaves. These findings enable the degree of resistance to virus multiplication to be quantified for the use of gene manipulation and breeding.

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Die Glucose-6-phosphat Dehydrogenase im Stoffwechsel photoautotropher Organismen

Cited by 11 publications

References 114 publications

Kinetic and electrophoretic characterization of NADP dependent dehydrogenases from root tissues of Norway spruce [Picea abies (L.) Karst.] employing a rapid one-step extraction procedure

Kinetic and electrophoretic characterization of NADP dependent dehydrogenases from root tissues of Norway spruce [Picea abies (L.) Karst.] employing a rapid one-step extraction procedure

Purification and Characterization of Two Isoforms of Glucose 6-Phosphate Dehydrogenase (G6PDH) fromChlorella vulgarisC-27

Correlation of viral RNA biosynthesis with glucose-6-phosphate dehydrogenase activity and host resistance

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