APHO1 from the yeast Arxula adeninivorans encodes an acid phosphatase of broad substrate specificity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-01

AUTHORS

Parvinder Kaur, Anja Lingner, Bijinder Singh, Erik Böer, Jelena Polajeva, Gerhard Steinborn, Rüdiger Bode, Gerd Gellissen, Tulasi Satyanarayana, Gotthard Kunze

ABSTRACT

The extracellular acid phosphatase-encoding Arxula adeninivorans APHO1 gene was isolated using degenerated specific oligonucleotide primers in a PCR screening approach. The gene harbours an ORF of 1449 bp encoding a protein of 483 amino acids with a calculated molecular mass of 52.4 kDa. The sequence includes an N-terminal secretion sequence of 17 amino acids. The deduced amino acid sequence exhibits 54% identity to phytases from Aspergillus awamori, Asp. niger and Asp. ficuum and a more distant relationship to phytases of the yeasts Candida albicans and Debaryomyces hansenii (36-39% identity). The sequence contains the phosphohistidine signature and the conserved active site sequence of acid phosphatases. APHO1 expression is induced under conditions of phosphate limitation. Enzyme isolates from wild and recombinant strains with the APHO1 gene expressed under control of the strong A. adeninivorans-derived TEF1 promoter were characterized. For both proteins, a molecular mass of approx. 350 kDa, corresponding to a hexameric structure, a pH optimum of pH 4.8 and a temperature optimum of 60 degrees C were determined. The preferred substrates include p-nitrophenyl-phosphate, pyridoxal-5-phosphate, 3-indoxyl-phosphate, 1-naphthylphosphate, ADP, glucose-6-phosphate, sodium-pyrophosphate, and phytic acid. Thus the enzyme is a secretory acid phosphatase with phytase activity and not a phytase as suggested by strong homology to such enzymes. More... »

PAGES

45-55

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s10482-006-9094-6

    DOI

    http://dx.doi.org/10.1007/s10482-006-9094-6

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1039639103

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/17016743


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