[23] Glucose 6-phosphate dehydrogenase (crystalline) from brewers' yeast

Kuby, Stephen A.; Noltmann, Ernst A.

doi:10.1016/0076-6879(66)09029-3

Cited by 87 publications

(34 citation statements)

References 4 publications

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“…Glucose-6-phosphate dehydrogenase activity [51] was absent in the mutant strain due to the ZWF1 gene disruption and was unchanged in the parental strain prior to and after the medium shift. NADP + -specific isocitrate dehydrogenase activity [15] was reduced ~four-fold in the mutant strain relative to the parental strain due to loss of Idp2p; these activities did not change as a function of the medium shift.…”

Section: Enzyme Activity Assaysmentioning

confidence: 95%

Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

Minard

Carroll

Weintraub

et al. 2007

Free Radical Biology and Medicine

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A yeast mutant lacking the two major cytosolic sources of NADPH, glucose-6-phosphate dehydrogenase (Zwf1p) and NADP + -specific isocitrate dehydrogenase (Idp2p), has been demonstrated to lose viability when shifted to medium with acetate or oleate as the carbon source. This loss in viability was found to correlate with an accumulation of endogenous oxidative byproducts of respiration and peroxisomal β-oxidation. To assess effects on cellular protein of endogenous versus exogenous oxidative stress, a proteomics approach was used to compare disulfide bondcontaining proteins in the idp2Δzwf1Δ strain following shifts to acetate and oleate media with those in the parental strain following similar shifts to media containing hydrogen peroxide. Among prominent disulfide bond-containing proteins were several with known antioxidant functions. These and several other proteins were detected as multiple electrophoretic isoforms, with some isoforms containing disulfide bonds under all conditions and other isoforms exhibiting a redox-sensitive content of disulfide bonds, i.e., in the idp2Δzwf1Δ strain and in the hydrogen peroxide-challenged parental strain. The disulfide bond content of some isoforms of these proteins was also elevated in the parental strain grown on glucose, possibly suggesting a redirection of NADPH reducing equivalents to support rapid growth. Further examination of protein carbonylation in the idp2Δzwf1Δ strain shifted to oleate medium also led to identification of common and unique protein targets of endogenous oxidative stress.

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Section: Enzyme Activity Assaysmentioning

confidence: 95%

Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

Minard

Carroll

Weintraub

et al. 2007

Free Radical Biology and Medicine

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show abstract

“…Enzymatic activities were determined following the methods established by Smith et al, (1988) for GLR; Holmgren & Björnstedt (1995) for TRR; Kuby & Noltmann (1966) for G6PDH and Aebi (1984) for CAT. All protocols, with the exception of CAT, were scaled down to reduce the final volume in order to measure absorbance in a 96-well microplate, using a GENios spectrophotometer (TECAN).…”

Section: Determination Of Enzymatic Activitiesmentioning

confidence: 99%

The Yeast Genes ROX1, IXR1, SKY1 and Their Effect upon Enzymatic Activities Related to Oxidative Stress

Leiro¹,

Lombardero²,

Vázquez³

et al. 2012

Oxidative Stress - Molecular Mechanisms and Biological Effects

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“…The procedure for preparation of homogenate for enzymes assay was estimated according to Bajpai et al (1981) and the assay methods for each enzyme are as follows; Hexokinase (EC 2.7.1.1) was assayed in 0.1 M glycylglycine buffer, pH 9.0 ( Darrow and Colowick, 1962), 6-phosphogluconate dehydrogenase (EC 1.1.1.44) in 0.1 M triethanolamina/HCl buffer, pH 7.6 ( Pontremoli and Grazi, 1966), glucose-6-phosphate dehydrogenase (EC 1.1.1.49) in 0.1 M glycylglycine buffer, pH 8.0 ( Kuby and Noltmann, 1966), glucose dihydrogenase (EC 1.1.1.47) in 0.1 M phosphate buffer, pH 6.0 (Hauge, 1966), gluconate dehydrogenase (EC 1.1.99.3) in 0.5 M sodium acetate buffer, pH 5.5 (Wood et al, 1962). One unit of enzyme activity was defined as the amount of enzyme, which catalysed the conversion of 1 µmol substrate into product minG 1 .…”

Section: Enzyme Assaysmentioning

confidence: 99%

Influence of pH on Kojic Acid Fermentation by Aspergillus flavus

Mohamad¹,

Ariff²,

Hassan³

et al. 2000

Pakistan J. of Biological Sciences

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Abstract:The influence of pH on kojic acid fermentation by Aspergillus flavus Link 44-1 in submerged fermentation and resuspended cell system was investigated separately. Although the highest growth in submerged fermentation was obtained at initial culture pH between 6 to 7, the optimum kojic acid production was achieved at initial culture pH 3. At initial culture pH 2, growth was greatly inhibited and kojic acid was not produced. In resuspended cell system using buffered glucose solution, in which the production of cell material was carried out at initial culture pH 3, the optimum kojic acid production was also obtained at pH 3. Kojic acid production in fermentation using 50 L stirred tank fermenter with pH control strategy (fermentation was started with pH 3 and without pH control during growth phase and culture pH was controlled at 3 during the production phase) was improved by about 20% as compared to fermentation without pH control. The maximum kojic acid concentration in fermentation with pH control strategy was 62.00 g/L and this gave yield and productivity of 0.516 g/g and 0.22 G/L h, respectively.

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[23] Glucose 6-phosphate dehydrogenase (crystalline) from brewers' yeast

Cited by 87 publications

References 4 publications

Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

The Yeast Genes ROX1, IXR1, SKY1 and Their Effect upon Enzymatic Activities Related to Oxidative Stress

Influence of pH on Kojic Acid Fermentation by Aspergillus flavus

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