Purification and properties of a glycoprotein acid phosphatase from the yeast form ofYarrowia lipolytica
Author:
Publisher
Wiley
Subject
Applied Microbiology and Biotechnology,General Medicine
Reference44 articles.
1. The nucleotide sequence of the yeastPHO5gene: a putative precursor of repressible acid phosphatase contains a signal peptide
2. 1981. Enzymes. In: Yeast Cell Envelopes: Biochemistry. Biophysics, and Ultrastructure (ed.), vol. II. Boca Raton, Florida: CRC Press, pp. 1 to 46.
3. Structural analysis of the two tandemly repeated acid phosphatase genes in yeast
4. PHO5 Upstream sequences confer phosphate control on the constitutivePHO3 gene
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1. Yarrowia lipolytica in Biotechnological Applications;SpringerBriefs in Microbiology;2014
2. Yeast Acid Phosphatases and Phytases: Production, Characterization and Commercial Prospects;Yeast Biotechnology: Diversity and Applications;2009
3. Characterization of major protein phosphatases from selected species ofKluyveromyces. Comparison with protein phosphatases fromYarrowia lipolytica;Canadian Journal of Microbiology;2001-09-01
4. The KIPHO5 gene encoding a repressible acid phosphatase in the yeast Kluyveromyces lactis: cloning, sequencing and transcriptional analysis of the gene, and purification and properties of the enzyme;Microbiology;1997-08-01
5. Purification and characterization of a type 2A protein phosphatase from Yarrowia lipolytica grown on a phosphate-deficient medium;Comptes Rendus de l'Académie des Sciences - Series III - Sciences de la Vie;1997-06
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