PMID: 8600983Mar 15, 1996Paper

Regulation of UDPG-pyrophosphorylase isoforms in Saccharomyces cerevisiae and their roles in trehalose metabolism

Biochimica Et Biophysica Acta
M B DutraA D Panek

Abstract

UDPG-pyrophosphorylase (EC 2.7.7.9) from Saccharomyces cerevisiae was studied and the presence of isoforms investigated. Its activity was monitored during growth of cultures in rich media containing glucose, galactose, sucrose, maltose or glycerol as carbon sources. The results suggest that UDPG-pyrophosphorylase is subject to both catabolite repression and catabolite inactivation. The inactivation process seems to be complex: in order to produce maximum inactivation, glucose and ammonium sulfate must be added together. Addition of glucose or ammonium sulfate separately produced little effect upon enzyme activity. Adsorption to and elution from a DEAE-Sephacel column of a crude protein extract prepared from yeast cells collected in stationary phase from a glucose medium showed three activity peaks, which we denominated isoform I, II, and III. Isoform I is constitutive, it was the only form present during exponential growth on glucose medium, and did not suffer any alteration after glucose exhaustion, heat shock or by growing cells on maltose. On the other hand, isoforms II and III were shown to be repressed by glucose, and induced by heat shock. Furthermore, isoform II of UDPG-pyrophosphorylase was present together with isoform...Continue Reading

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Citations

Jun 21, 2011·Applied and Environmental Microbiology·Yongqin JiaoMichael P Thelen
Jun 29, 2004·Biochemical and Biophysical Research Communications·Wayne A WilsonPeter J Roach
Aug 30, 2014·Critical Reviews in Microbiology·Yang LiZhen-Ming Chi
May 29, 2007·Molecular Cell·Tammy L Smith, Jared Rutter
Feb 23, 2020·Microbial Cell Factories·Weihua NanWenyu Lu

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