1977
DOI: 10.1099/00221287-102-2-391
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Pathways of Glucose Metabolism in Candida 107, a Lipid-accumulating Yeast

Abstract: Phosphofructokinase was not detected in extracts of Candida 107 prepared in a variety of ways but was highly active in cells treated with toluene. Disruption of these cells destroyed activity of phosphofructokinase indicating that the enzyme is extremely labile. As patterns of labelling from [~-~~C]glucose and [6-14C]glucose showed that 60 % of glucose was metabolized via the pentose cycle, augmentation of this cycle is necessary to account for the high molar growth yields of this yeast. Phosphoketolases, reac… Show more

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Cited by 25 publications
(22 citation statements)
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“…However, we did find an active, though extremely labile, phosphofructokinase in both these yeasts and, from isotope-labelling studies with Candida 107, calculated that about 65% of the glucose as growth substrate was being metabolized via the pentose phosphate cycle, with the remainder going through the Embden-Meyerhof pathway (Ratledge & Botham, 1977). In both yeasts, these two pathways of glucose dissimilation were augmented to an unknown extent by hexose-and pentose-phosphoketolase(s) (Whitworth & which would serve to produce acetyl-CoA directly from glucose in the cytoplasm rather than in the mitochondria as usually happens.…”
Section: P a Botham A N D C Ratledgementioning
confidence: 99%
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“…However, we did find an active, though extremely labile, phosphofructokinase in both these yeasts and, from isotope-labelling studies with Candida 107, calculated that about 65% of the glucose as growth substrate was being metabolized via the pentose phosphate cycle, with the remainder going through the Embden-Meyerhof pathway (Ratledge & Botham, 1977). In both yeasts, these two pathways of glucose dissimilation were augmented to an unknown extent by hexose-and pentose-phosphoketolase(s) (Whitworth & which would serve to produce acetyl-CoA directly from glucose in the cytoplasm rather than in the mitochondria as usually happens.…”
Section: P a Botham A N D C Ratledgementioning
confidence: 99%
“…The incorporation of radioactivity from [ l-14C]acetate was a measure of acetyl-CoA carboxylase and was not limited by the activity of acetyl-CoA synthetase which, being about 1.0 pmol h-l (mg protein)-l in both yeasts, was an order of magnitude higher than the activity of acetylCoA carboxylase. [Although there was a low activity of acetate kinase in both yeasts, there was no activity of phosphate acetyltransferase (see Ratledge & Botham, 1977) indicating that synthesis of acetyl-CoA was solely via acetyl-CoA synthetase.] The K, values for acetyl-CoA, calculated in the usual manner, were 4 mM in Candida 107 and 3 mM in C. utilis.…”
Section: Regulation Of Glucose Transportmentioning
confidence: 99%
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