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Volumn 65, Issue 2, 1999, Pages 359-366

Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): Molecular size, glycosylation pattern, and engineering of proteolytic resistance

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATE; PHYTASE;

EID: 0032976125     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.65.2.359-366.1999     Document Type: Article
Times cited : (182)

References (33)
  • 1
    • 0013801195 scopus 로고
    • The gel-filtration behaviour of proteins related to their molecular weights over a wide range
    • Andrews, P. 1965. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem. J. 96:595-606.
    • (1965) Biochem. J. , vol.96 , pp. 595-606
    • Andrews, P.1
  • 2
    • 0025007533 scopus 로고
    • The complete nucleotide sequence of the Escherichia coli gene appA reveals significant homology between pH 2.5 acid phosphatase and glucose-1-phosphatase
    • Dassa, J., C. Marck, and P. L. Boquet. 1990. The complete nucleotide sequence of the Escherichia coli gene appA reveals significant homology between pH 2.5 acid phosphatase and glucose-1-phosphatase. J. Bacteriol. 172:5497-5500.
    • (1990) J. Bacteriol. , vol.172 , pp. 5497-5500
    • Dassa, J.1    Marck, C.2    Boquet, P.L.3
  • 5
    • 0023957340 scopus 로고
    • Purification and characterization of phytase from cotyledons of germinating soybean seeds
    • Gibson, D. M., and A. H. J. Ullah. 1988. Purification and characterization of phytase from cotyledons of germinating soybean seeds. Arch. Biochem. Biophys. 260:503-513.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 503-513
    • Gibson, D.M.1    Ullah, A.H.J.2
  • 6
    • 0027208581 scopus 로고
    • Purification and characterization of two phytases from Escherichia coli
    • Greiner, R., U. Konietzny, and K.-D. Jany. 1993. Purification and characterization of two phytases from Escherichia coli. Arch. Biochem. Biophys. 303:107-113.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 107-113
    • Greiner, R.1    Konietzny, U.2    Jany, K.-D.3
  • 7
    • 0031570310 scopus 로고    scopus 로고
    • Purification and characterization of a phytase from Klebsiella terrigena
    • Greiner, R., E. Haller, U. Konietzny, and K.-D. Jany. 1997. Purification and characterization of a phytase from Klebsiella terrigena. Arch. Biochem. Biophys. 341:201-206.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 201-206
    • Greiner, R.1    Haller, E.2    Konietzny, U.3    Jany, K.-D.4
  • 8
    • 0030451745 scopus 로고    scopus 로고
    • Deglycosylation of proteins for crystallization using recombinant fusion protein glycosidases
    • Grueninger-Leitch, F., A. D'Arcy, B. D'Arcy, and C. Chène. 1996. Deglycosylation of proteins for crystallization using recombinant fusion protein glycosidases. Protein Sci. 5:2617-2622.
    • (1996) Protein Sci. , vol.5 , pp. 2617-2622
    • Grueninger-Leitch, F.1    D'Arcy, A.2    D'Arcy, B.3    Chène, C.4
  • 10
    • 0030478075 scopus 로고    scopus 로고
    • Maize root phytase
    • Hübel, F., and E. Beck. 1996. Maize root phytase. Plant Physiol. 112:1429-1436.
    • (1996) Plant Physiol. , vol.112 , pp. 1429-1436
    • Hübel, F.1    Beck, E.2
  • 11
    • 0028816805 scopus 로고
    • Influence of carbohydrate on structure, stability, and function of gelatin-binding fragments of fibronectin
    • Ingham, K. C., S. A. Brew, and V. V. Novokhatny. 1995. Influence of carbohydrate on structure, stability, and function of gelatin-binding fragments of fibronectin. Arch. Biochem. Biophys. 316:235-240.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 235-240
    • Ingham, K.C.1    Brew, S.A.2    Novokhatny, V.V.3
  • 12
    • 0024986340 scopus 로고
    • The influence of GAP promoter variants on hirudin production, average plasmid copy number and cell growth in Saccharomyces cerevisiae
    • Janes, M., B. Meyhack, W. Zimmermann, and A. Hinnen. 1990. The influence of GAP promoter variants on hirudin production, average plasmid copy number and cell growth in Saccharomyces cerevisiae. Curr. Genet. 18:97-103.
    • (1990) Curr. Genet. , vol.18 , pp. 97-103
    • Janes, M.1    Meyhack, B.2    Zimmermann, W.3    Hinnen, A.4
  • 14
    • 0031034203 scopus 로고    scopus 로고
    • The phytase subfamily of histidine acid phosphatases: Isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila
    • Mitchell, D. B., K. Vogel, B. Weimann, L. Pasamontes, and A. P. G. M. van Loon. 1997. The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila. Microbiology 143:245-252.
    • (1997) Microbiology , vol.143 , pp. 245-252
    • Mitchell, D.B.1    Vogel, K.2    Weimann, B.3    Pasamontes, L.4    Van Loon, A.P.G.M.5
  • 15
    • 0030898612 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus
    • Pasamontes, L., M. Haiker, M. Wyss, M. Tessier, and A. P. G. M. van Loon. 1997. Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus. Appl. Environ. Microbiol. 63:1696-1700.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1696-1700
    • Pasamontes, L.1    Haiker, M.2    Wyss, M.3    Tessier, M.4    Van Loon, A.P.G.M.5
  • 17
    • 0023512725 scopus 로고
    • Transformation of Aspergillus based on the hygromycin B resistance marker from Escherichia coli
    • Punt, P. J., R. P. Oliver, M. A. Dingemanse, P. H. Pouwels, and C. A. M. J. J. van den Hondel. 1987. Transformation of Aspergillus based on the hygromycin B resistance marker from Escherichia coli. Gene 56:117-124.
    • (1987) Gene , vol.56 , pp. 117-124
    • Punt, P.J.1    Oliver, R.P.2    Dingemanse, M.A.3    Pouwels, P.H.4    Van Den Hondel, C.A.M.J.J.5
  • 19
    • 0028921674 scopus 로고
    • The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator
    • Rudd, P. M., R. J. Woods, M. R. Wormald, G. Opdenakker, A. K. Downing, I. D. Campbell, and R. A. Dwek. 1995. The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator. Biochim. Biophys. Acta 1248:1-10.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 1-10
    • Rudd, P.M.1    Woods, R.J.2    Wormald, M.R.3    Opdenakker, G.4    Downing, A.K.5    Campbell, I.D.6    Dwek, R.A.7
  • 20
    • 0027928436 scopus 로고
    • Simultaneous radial and wavelength analysis with the Optima XL-A analytical centrifuge
    • Schuck, P. 1994. Simultaneous radial and wavelength analysis with the Optima XL-A analytical centrifuge. Prog. Colloid Polym. Sci. 94:1-13.
    • (1994) Prog. Colloid Polym. Sci. , vol.94 , pp. 1-13
    • Schuck, P.1
  • 22
    • 0000666697 scopus 로고
    • Purification and characterization of phytase from Bacillus subtilis (natto) N-77
    • Shimizu, M. 1992. Purification and characterization of phytase from Bacillus subtilis (natto) N-77. Biosci. Biotechnol. Biochem. 56:1266-1269.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 1266-1269
    • Shimizu, M.1
  • 23
    • 84925491834 scopus 로고
    • Purification and characterization of phytase and acid phosphatase produced by Aspergillus oryzae K1
    • Shimizu, M. 1993. Purification and characterization of phytase and acid phosphatase produced by Aspergillus oryzae K1. Biosci. Biotechnol. Biochem. 57:1364-1365.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1364-1365
    • Shimizu, M.1
  • 24
    • 0344026086 scopus 로고    scopus 로고
    • Unpublished data
    • Tomschy, A. Unpublished data.
    • Tomschy, A.1
  • 26
    • 0016167677 scopus 로고
    • Beta-galactosidase from termination and deletion mutant strains
    • Villarejo, M. R., and J. Zabin. 1974. Beta-galactosidase from termination and deletion mutant strains. J. Bacteriol. 120:466-476.
    • (1974) J. Bacteriol. , vol.120 , pp. 466-476
    • Villarejo, M.R.1    Zabin, J.2
  • 27
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • von Heijne, G. 1983. Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 133:17-21.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 28
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 29
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • Wang, C., M. Eufemi, C. Turano, and A. Giartosio. 1996. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 35:7299-7307.
    • (1996) Biochemistry , vol.35 , pp. 7299-7307
    • Wang, C.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 31
    • 0031734945 scopus 로고    scopus 로고
    • Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. Niger phytase, and A niger pH 2.5 acid phosphatase
    • Wyss, M., L. Pasamontes, R. Rémy, J. Kohler, E. Kusznir, M. Gadient, F. Müller, and A. P. G. M. van Loon. 1998. Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase, and A niger pH 2.5 acid phosphatase. Appl. Environ. Microbiol. 64:4446-4451.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4446-4451
    • Wyss, M.1    Pasamontes, L.2    Rémy, R.3    Kohler, J.4    Kusznir, E.5    Gadient, M.6    Müller, F.7    Van Loon, A.P.G.M.8
  • 33
    • 0000628063 scopus 로고
    • Chemical and physicochemical properties of phytase from Aspergillus terreus
    • Yamamoto, S., Y. Minoda, and K. Yamada. 1972. Chemical and physicochemical properties of phytase from Aspergillus terreus. Agric. Biol. Chem. 36:2097-2103.
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 2097-2103
    • Yamamoto, S.1    Minoda, Y.2    Yamada, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.