PMID: 7011403Feb 13, 1981Paper

A particulate form of alkaline phosphatase in the yeast, Saccharomyces cerevisiae

Biochimica Et Biophysica Acta
J K MitchellD J Opheim

Abstract

A new form of alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) has been identified in the yeast Saccharomyces cerevisiae. Utilizing either synthetic or natural substrates, the enzyme exhibited a broad pH activity curve with maximum activity between 8.5 and 9.0. The enzyme was nonspecific with respect to substrate, attacking a variety of compounds containing phosphomonoester linkages, but has no detectable activity against polyphosphate, pyrophosphate or phosphodiester linkages. The enzyme exhibited an apparent Km of 0.25 mM with respect to p-nitrophenyl phosphate, 0.38 mM with respect to alpha-naphthyl phosphate, and 1.0 mM with respect to 5'AMP. The enzyme is regulated in a constitutive manner and its activity does not increase during phosphate starvation or sporulation, as does the repressible alkaline phosphatase. The enzyme is tightly bound to a particulate fraction of the cell, tentatively identified as the tonoplast membrane. It is not solubilized by treatment with high concentrations of NaCl, KH2PO4 or chaotropic agents. Triton X-100 (0.1%) solubilizes 12% of the particulate activity. This enzyme is differentiated from the other alkaline phosphatases found in yeast by its c...Continue Reading

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Citations

May 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·J H RothmanT H Stevens
Jul 1, 1994·The Journal of Cell Biology·A HaasW Wickner
Mar 1, 1996·The Journal of Cell Biology·Z Xu, W Wickner
Dec 22, 2007·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·J FernandesM J Martins
Jan 1, 1993·Critical Reviews in Biotechnology·K Murata
Jun 1, 1996·Molecular and Cellular Biology·S F NothwehrT H Stevens
Sep 1, 1990·Microbiological Reviews·D J KlionskyS D Emr

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