메뉴 건너뛰기




Volumn 328, Issue 2, 2005, Pages 404-408

Conservation of cysteine residues in fungal histidine acid phytases

Author keywords

Bioinformatics; BLAST; Cysteine; Disulfide bridge; Enzyme stability; Histidine acid phosphatase; Phytase

Indexed keywords

CYSTEINE DERIVATIVE; FUNGAL PROTEIN; HISTIDINE; PHYTASE; POLYPEPTIDE;

EID: 13444293033     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.12.181     Document Type: Article
Times cited : (23)

References (27)
  • 1
    • 0034030803 scopus 로고    scopus 로고
    • Impacts of industrial animal production on rivers and estuaries
    • M.A. Mallin Impacts of industrial animal production on rivers and estuaries Am. Sci. 88 2000 26 27
    • (2000) Am. Sci. , vol.88 , pp. 26-27
    • Mallin, M.A.1
  • 3
    • 0031986622 scopus 로고    scopus 로고
    • Phytase: Sources, preparation and exploitation
    • J. Dvorakova Phytase: sources, preparation and exploitation Folia Microbiol. 43 1998 323 338
    • (1998) Folia Microbiol. , vol.43 , pp. 323-338
    • Dvorakova, J.1
  • 5
    • 1642578253 scopus 로고    scopus 로고
    • Biochemical properties and substrate specificities of alkaline and histidine acid phytases
    • B.C. Oh, W.C. Choi, S. Park, Y.O. Kim, and T.K. Oh Biochemical properties and substrate specificities of alkaline and histidine acid phytases Appl. Microbiol Biotechnol. 63 2004 362 372
    • (2004) Appl. Microbiol Biotechnol. , vol.63 , pp. 362-372
    • Oh, B.C.1    Choi, W.C.2    Park, S.3    Kim, Y.O.4    Oh, T.K.5
  • 6
    • 0036392430 scopus 로고    scopus 로고
    • In vitro properties of phytases from various microbial origins
    • O. Simon, and F. Igbasan In vitro properties of phytases from various microbial origins Int. J. Food Sci. Tech. 37 2002 813 822
    • (2002) Int. J. Food Sci. Tech. , vol.37 , pp. 813-822
    • Simon, O.1    Igbasan, F.2
  • 7
    • 0025787109 scopus 로고
    • Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytases
    • A.H.J. Ullah, B.J. Cummins, and H.C. Dischinger Jr. Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytases Biochem. Biophys. Res. Commun. 178 1991 45 53
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 45-53
    • Ullah, A.H.J.1    Cummins, B.J.2    Dischinger Jr., H.C.3
  • 8
    • 0025915380 scopus 로고
    • Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase
    • R.L. Van Etten, R. Davidson, P.E. Stevis, H. MacArthur, and D.L. Moore Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase J. Biol. Chem. 266 1991 2313 2319
    • (1991) J. Biol. Chem. , vol.266 , pp. 2313-2319
    • Van Etten, R.L.1    Davidson, R.2    Stevis, P.E.3    MacArthur, H.4    Moore, D.L.5
  • 10
    • 2342501800 scopus 로고    scopus 로고
    • Crystal structure of a heat-resilient phytases from Aspergillus fumigatus, carrying a phosphorylated histidine
    • T. Xiang, Q. Liu, A.M. Deacon, M. Koshy, I.A. Kriksunov, X.G. Lei, Q. Hao, and D.J. Thiel Crystal structure of a heat-resilient phytases from Aspergillus fumigatus, carrying a phosphorylated histidine J. Mol. Biol. 339 2004 437 445
    • (2004) J. Mol. Biol. , vol.339 , pp. 437-445
    • Xiang, T.1    Liu, Q.2    Deacon, A.M.3    Koshy, M.4    Kriksunov, I.A.5    Lei, X.G.6    Hao, Q.7    Thiel, D.J.8
  • 11
    • 0033591464 scopus 로고    scopus 로고
    • Crystal Structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4 a resolution
    • D. Kostrewa, M. Wyss, A. D'Arcy, and A.P.G.M. van Loon Crystal Structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4 A resolution J. Mol. Biol. 288 1999 965 974
    • (1999) J. Mol. Biol. , vol.288 , pp. 965-974
    • Kostrewa, D.1    Wyss, M.2    D'Arcy, A.3    Van Loon, A.P.G.M.4
  • 12
    • 0030583553 scopus 로고    scopus 로고
    • Disulfide bonds are necessary for structure and activity in Aspergillus ficuum phytases (phyA)
    • A.H.J. Ullah, and E.J. Mullaney Disulfide bonds are necessary for structure and activity in Aspergillus ficuum phytases (phyA) Biochem. Biophys. Res. Commun. 227 1996 311 317
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 311-317
    • Ullah, A.H.J.1    Mullaney, E.J.2
  • 13
    • 2542483890 scopus 로고    scopus 로고
    • The role of disulfide bonds in the conformational stability and catalytic activity of phytase
    • X. Wang, F. Meng, and H. Zhou The role of disulfide bonds in the conformational stability and catalytic activity of phytase Biochem. Cell Biol. 82 2004 329 334
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 329-334
    • Wang, X.1    Meng, F.2    Zhou, H.3
  • 14
    • 0029052528 scopus 로고
    • Molecular cloning, expression and evaluation of phosphohydrolases for phytate-degrading activity
    • E. Moore, V.R. Helly, O.M. Conneely, P.P. Ward, R.F. Power, and D.R. Headon Molecular cloning, expression and evaluation of phosphohydrolases for phytate-degrading activity J. Ind. Microbiol. 14 1995 396 402
    • (1995) J. Ind. Microbiol. , vol.14 , pp. 396-402
    • Moore, E.1    Helly, V.R.2    Conneely, O.M.3    Ward, P.P.4    Power, R.F.5    Headon, D.R.6
  • 15
    • 85030819330 scopus 로고    scopus 로고
    • Method for producing phytase, Patent: EP 0931837-A, 28 July, 1999
    • D. Mochizuki, H. Takahashi, Method for producing phytase, Patent: EP 0931837-A, 28 July, 1999
    • Mochizuki, D.1    Takahashi, H.2
  • 16
    • 0038235596 scopus 로고    scopus 로고
    • Immobilization of Candida krusei cells producing phytases in alginate gel beads: An application of the preparation of myo-inositol phosphates
    • C.S. Quan, S.D. Fan, and Y. Ohta Immobilization of Candida krusei cells producing phytases in alginate gel beads: an application of the preparation of myo-inositol phosphates Appl. Microbiol. Biotechnol. 62 2003 41 47
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , pp. 41-47
    • Quan, C.S.1    Fan, S.D.2    Ohta, Y.3
  • 17
    • 85047683976 scopus 로고    scopus 로고
    • Expression, gene cloning and characterization of five novel phytases from four basidomycete fungi: Peniophora lycii, Agrocybe pediades, a Ceriporia sp., and Trametes pubescens
    • S.F. Lassen, J. Breinholt, P.R. Ostergaard, R. Brugger, A. Bischoff, M. Wyss, and C.C. Fuglsang Expression, gene cloning and characterization of five novel phytases from four basidomycete fungi: Peniophora lycii, Agrocybe pediades, a Ceriporia sp., and Trametes pubescens Appl. Environ. Microbiol. 67 2001 4701 4707
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4701-4707
    • Lassen, S.F.1    Breinholt, J.2    Ostergaard, P.R.3    Brugger, R.4    Bischoff, A.5    Wyss, M.6    Fuglsang, C.C.7
  • 18
    • 3242886780 scopus 로고    scopus 로고
    • GDAP: A web tool for genome-wide protein disulfide bond prediction
    • B.D. O'Conner, and T.O. Yeates GDAP: a web tool for genome-wide protein disulfide bond prediction Nucleic Acids Res. 32 2004 w360 w364
    • (2004) Nucleic Acids Res. , vol.32
    • O'Conner, B.D.1    Yeates, T.O.2
  • 20
    • 0031734945 scopus 로고    scopus 로고
    • Comparison of the thermostability properties of three acid phosphatase from molds: Aspergillus fumigatus phytase, A. niger phytase, and A. niger pH 2.5 acid phosphatase
    • M. Wyss, L. Pasamontes, R. Remy, J. Kohler, E. Kusznir, M. Gadient, F. Muller, and A.P.G.M. van Loon Comparison of the thermostability properties of three acid phosphatase from molds: Aspergillus fumigatus phytase, A. niger phytase, and A. niger pH 2.5 acid phosphatase Appl. Environ. Microbiol. 64 1998 4446 4451
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4446-4451
    • Wyss, M.1    Pasamontes, L.2    Remy, R.3    Kohler, J.4    Kusznir, E.5    Gadient, M.6    Muller, F.7    Van Loon, A.P.G.M.8
  • 21
    • 0023080759 scopus 로고
    • Extracellular phytase (E.C. 3.1.3.8) from Aspergillus ficuum NRRL 3135: Purification and characterization
    • A.H.J. Ullah, and D.M. Gibson Extracellular phytase (E.C. 3.1.3.8) from Aspergillus ficuum NRRL 3135: purification and characterization Prep. Biochem. 17 1987 63 91
    • (1987) Prep. Biochem. , vol.17 , pp. 63-91
    • Ullah, A.H.J.1    Gibson, D.M.2
  • 22
    • 0030898612 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus
    • L. Pasamontes, M. Haiker, M. Wyss, M. Tessier, and A.P.G.M. van Loon Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus Appl. Environ. Microbiol. 63 1997 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
  • 24
    • 0037246131 scopus 로고    scopus 로고
    • Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations
    • H. Lui, and W. Wang Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations PEDS 16 2003 19 25
    • (2003) PEDS , vol.16 , pp. 19-25
    • Lui, H.1    Wang, W.2
  • 25
    • 0034731381 scopus 로고    scopus 로고
    • The consensus concept for thermostability engineering of proteins
    • M. Lehmann, L. Pasamontes, S.F. Lassen, and M. Wyss The consensus concept for thermostability engineering of proteins Biochim. Biophys. Acta 1543 2000 408 415
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 408-415
    • Lehmann, M.1    Pasamontes, L.2    Lassen, S.F.3    Wyss, M.4
  • 26
    • 34248142878 scopus 로고    scopus 로고
    • Stability of plant and microbial phytases
    • R. Reddy S.K. Sathe Technomic Inc. Lancaster, PA
    • B.Q. Phillippy Stability of plant and microbial phytases R. Reddy S.K. Sathe Food Phytase 2000 Technomic Inc. Lancaster, PA 7 126
    • (2000) Food Phytase , pp. 7-126
    • Phillippy, B.Q.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.