Glucose-6-phosphate dehydrogenase from Dicentrarchus labrax liver: kinetic mechanism and kinetics of NADPH inhibition

Bautista, José M.; Garrido-Pertierra, Amando; Soler, Germán

doi:10.1016/0304-4165(88)90098-0

Cited by 86 publications

(40 citation statements)

References 39 publications

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“…Because approximately half of Tsa1 is continuously oxidized (Okazaki et al, 2007) at the expense of NADPH, the intracellular NADPH level of tsa1/2Δ cells might be higher than that of wild-type cells. However, glucose-6-phosphate dehydrogenase activity, which catalyzes the rate-limiting step of the pentose-phosphate pathway, is inhibited by NADPH (Bautista et al, 1992(Bautista et al, , 1988. The pentose phosphate pathway is required for the production of NADPH and essential molecules for cell growth, such as ribonucleotides.…”

Section: Discussionmentioning

confidence: 99%

Requirement of peroxiredoxin on the stationary phase of yeast cell growth

et al. 2014

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-Toxic chemicals often induce reactive oxygen species (ROS). Although one of the most abundant ROS-sensitive proteins is in the peroxiredoxin (Prx) family, the function of Prx proteins is poorly understood because they are inactivated under high concentrations of hydrogen peroxide. Like mammalian cells, the model eukaryote Saccharomyces cerevisiae possesses multiple Prx proteins. Among the five Prx family proteins, Tsa1 and Ahp1 have the highest and second-highest expression levels, respectively. Here, we focused on a previously uncharacterized phenotype resulting from Tsa1 loss: impaired growth during the late exponential phase. We overexpressed catalase (CTT1) and Ahp1 in cells with disruptions in TSA1 and its homologue, TSA2 (tsa1/2Δ cells), and we found that neither Ctt1 nor Ahp1 overexpression suppressed the impaired cell growth at the stationary phase, although the ROS levels were successfully suppressed. Furthermore, the cell cycle profile was not altered by Tsa1/2 loss, at least in the late exponential phase; however, the glucose consumption rate slowed in the late exponential phase. Our results suggest that ROS levels are not responsible for the growth phenotype. Tsa1 might have a specific function that could not be replaced by Ahp1.

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Section: Discussionmentioning

confidence: 99%

Requirement of peroxiredoxin on the stationary phase of yeast cell growth

et al. 2014

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“…Soluble protein content of the liver was determined on supernatant by the method of Bradford (1976) using bovine serum albumin (BSA) as standard. Selected lipogenic enzyme activities were assayed on the supernatant using spectrophotometric procedures: G6PD (EC 1.1.1.49) according to Bautista et al(1988), ME (EC 1.1.1.40) according to Ochoa (1955) and FAS (EC 2.3.1.38) according to the methodology of Chang et al(1967) as modified by Chakrabarty and Leveille (1969). One unit (U) of enzyme activity, defined as mmoles of substrate converted to product per min at assay temperature, expressed 1 mg of hepatic soluble protein specific activity.…”

Section: Enzyme Assaysmentioning

confidence: 99%

Influence of dietary conjugated linoleic acid on growth, fatty acid composition and hepatic lipogenesis in large yellow croaker (Pseudosciaena crocea R.)

Zhao

Tang

et al. 2008

J. Zhejiang Univ. Sci. B

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Zhao et al. / J Zhejiang Univ Sci B 2008 9(9)Abstract: We examined the effects of conjugated linoleic acid (CLA) on growth, fatty acid composition and enzyme activity of fatty acid oxidation in the liver of large yellow croaker. We divided 1600 fish (average initial weight 150 g) into 4 groups and reared them in 8 cages. Four dietary treatments were formulated to contain 0%, 1%, 2% and 4% (w/w) CLA, respectively. The fish were fed for 10 weeks ad libitum twice daily. We found that the dietary CLA had no effect on growth, biometric parameters and whole body proximate (P>0.05), but showed some significant effects on the fatty acid composition in both muscle and the liver. The activities of lipogenic enzymes were slightly depressed in fish fed with increasing levels of CLA when compared with control (P>0.05). Dietary CLA supplementation had no effects on liver lipid content, but significantly increased the contents of saturated fatty acids (SFA) and polyunsaturated fatty acids (PUFA) (P<0.05) and decreased monounsaturated fatty acid (MUFA) content in both muscle and the liver. Dietary CLA inclusion resulted in significant increases of the biologically active cis-9, trans-11 and trans-10, cis-12 isomers in both tissues (P<0.05). The total accumulation of CLA was higher in the liver (3.83%, w/w) than in muscle (3.77%, w/w) when fed with 4% (w/w) CLA. This study demonstrates that large yellow croakers are capable of absorbing and depositing CLA and long-chain n-3 PUFA in the liver and muscle, showing that this species fed with CLA could be an important human food source for these healthful fatty acids.

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“…On the contrary, higher intracellular NADPH demand, as occurs under stress conditions, led to the specific disappearance of the faster-migrating G6PDH band (Fig. 7), confirming its role as an inhibitory component of G6PDH to avoid toxic accumulation of NADPH (4).…”

Section: Discussionmentioning

confidence: 60%

“…In S. cerevisiae, it has been reported that pgi1 mutants are unable to grow on glucose because diversion of the glycolytic flux toward the PPP leads to a toxic accumulation of NADPH that, by inhibiting G6PDH, may explain the observed cell growth arrest (7,23). Moreover, in Dicentrarchus labrax liver, it has also been reported that accumulation of NADPH in the cytosol may lead to inhibition of G6PDH activity (4).…”

Section: Figmentioning

confidence: 99%

Intracellular NADPH Levels Affect the Oligomeric State of the Glucose 6-Phosphate Dehydrogenase

et al. 2012

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In the yeast Kluyveromyces lactis, glucose 6-phosphate dehydrogenase (G6PDH) is detected as two differently migrating forms on native polyacrylamide gels. The pivotal metabolic role of G6PDH in K. lactis led us to investigate the mechanism controlling the two activities in respiratory and fermentative mutant strains. An extensive analysis of these mutants showed that the NAD ؉ (H)/NADP ؉ (H)-dependent cytosolic alcohol (ADH) and aldehyde (ALD) dehydrogenase balance affects the expression of the G6PDH activity pattern. Under fermentative/ethanol growth conditions, the concomitant activation of ADH and ALD activities led to cytosolic accumulation of NADPH, triggering an alteration in the oligomeric state of the G6PDH caused by displacement/release of the structural NADP ؉ bound to each subunit of the enzyme. The new oligomeric G6PDH form with fastermigrating properties increases as a consequence of intracellular redox unbalance/NADPH accumulation, which inhibits G6PDH activity in vivo. The appearance of a new G6PDH-specific activity band, following incubation of Saccharomyces cerevisiae and human cellular extracts with NADP ؉ , also suggests that a regulatory mechanism of this activity through NADPH accumulation is highly conserved among eukaryotes.

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Glucose-6-phosphate dehydrogenase from Dicentrarchus labrax liver: kinetic mechanism and kinetics of NADPH inhibition

Cited by 86 publications

References 39 publications

Requirement of peroxiredoxin on the stationary phase of yeast cell growth

Requirement of peroxiredoxin on the stationary phase of yeast cell growth

Influence of dietary conjugated linoleic acid on growth, fatty acid composition and hepatic lipogenesis in large yellow croaker (Pseudosciaena crocea R.)

Intracellular NADPH Levels Affect the Oligomeric State of the Glucose 6-Phosphate Dehydrogenase

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