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Digitale Medien

Presence of two trehalose-6-phosphate synthase enzymes in Candida utilis (1989)

Vicente-Soler, J. ; Arguelles, J.C. ; Gacto, M.

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 61 (1989), S. 0

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ISSN: 1574-6968

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Biologie

Notizen: Abstract Total trehalose-6-phosphate synthase activity decreased in cell extracts from Candida utilis under conditions inducing activation of the regulatory trehalase by protein kinase catalysed phosphorylation. The synthase activity was reactivated by treatment with alkaline phosphatase revealing the presence of an enzyme whose activity is inactivated by reversible phosphorylation. The occurrence in the trehalose-6-phosphate synthase complex of a second synthase enzyme whose activity is not controlled by phosphorylation and dephosphorylation was demonstrated following gel filtration of cell extracts. The activity of the isolated enzymes was differently modified in vitro by the presence of alkaline phosphatase, ATP, glucose or protein kinase.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03636.x

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Digitale Medien

Protein phosphorylation and trehalase activation in Candida utilis (1986)

Arguelles, J.C. ; Vicente-Soler, J. ; Gacto, M.

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 34 (1986), S. 0

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ISSN: 1574-6968

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Biologie

Notizen: Abstract Candida utilis cells contain a regulatory trehalase enzyme (280 kDa) which can be activated by cAMP-dependent phosphorylation. A 100-fold purification of this enzyme activity results in the enrichment of a protein band of apparent Mr 70 000 as identified by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). This component is phosphorylated in vivo under conditions in which trehalase activation occurs in whole cells. It is concluded that the trehalase enzyme might be a tetramer, composed of 4 identical 70-kDa subunits.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1574-6968.1986.tb01437.x

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Digitale Medien

Differential location of regulatory and nonregulatory trehalases inCandida utilis cells (1988)

Arguelles, J. C. ; Gacto, M.

Springer

Antonie van Leeuwenhoek 54 (1988), S. 555-565

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ISSN: 1572-9699

Schlagwort(e): trehalases ; vacuoles ; glycoproteins ; Candida utilis

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: Abstract The isolation of vacuoles by density gradient centrifugation of protoplast lysates fromCandida utilis cells showed a high specific activity for nonregulatory trehalase in vacuoles whereas the regulatory trehalase activatable by phosphorylation behaves as a cytoplasmic enzyme. The vacuolar trehalase is a glycoprotein that can be precipitated by Con A-Sepharose. Treatment of this enzyme with endo H reduced its reactivity with the lectin without loss of enzyme activity and decreased its apparent molecular weight by gel filtration.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00588391

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