메뉴 건너뛰기




Volumn 185, Issue 23, 2003, Pages 6780-6789

An Arsenate Reductase from Synechocystis sp. Strain PCC 6803 Exhibits a Novel Combination of Catalytic Characteristics

Author keywords

[No Author keywords available]

Indexed keywords

ARSENATE REDUCTASE; ARSENIC ACID; ARSENOCYSTEINE; CYSTEINE DERIVATIVE; GLUTAREDOXIN; GLUTATHIONE; OXIDOREDUCTASE; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 0344393487     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.23.6780-6789.2003     Document Type: Article
Times cited : (63)

References (57)
  • 1
    • 0035923503 scopus 로고    scopus 로고
    • Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases
    • Bennett, M. S., Z. Guan, M. Laurberg, and X.-D. Su. 2001. Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 98:13577-13582.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13577-13582
    • Bennett, M.S.1    Guan, Z.2    Laurberg, M.3    Su, X.-D.4
  • 2
    • 0030836016 scopus 로고    scopus 로고
    • Isolation of three contiguous genes, ACR1, ACR2, and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae
    • Bobrowicz, P., R. Wysocki, G. Owsianik, A. Goffeau, and S. Ulaszewski. 1997. Isolation of three contiguous genes, ACR1, ACR2, and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Yeast 13:819-828.
    • (1997) Yeast , vol.13 , pp. 819-828
    • Bobrowicz, P.1    Wysocki, R.2    Owsianik, G.3    Goffeau, A.4    Ulaszewski, S.5
  • 3
    • 0017184389 scopus 로고
    • A rapid and simple method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and simple method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0026799490 scopus 로고
    • Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14→S) and its mixed disulfide with glutathione
    • Bushweller, J. H., F. Aslund, K. Wuthrich, and A. Holmgren. 1992. Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14→S) and its mixed disulfide with glutathione. Biochemistry 31: 9288-9293.
    • (1992) Biochemistry , vol.31 , pp. 9288-9293
    • Bushweller, J.H.1    Aslund, F.2    Wuthrich, K.3    Holmgren, A.4
  • 6
    • 0034016916 scopus 로고    scopus 로고
    • The chromosomal arsenical resistance genes of Thiobacillus ferrooxidans have an unusual arrangement and confer increased arsenical resistance to Escherichia coli
    • Butcher, B. G., S. M. Deane, and D. R. E. Rawlings. 2000. The chromosomal arsenical resistance genes of Thiobacillus ferrooxidans have an unusual arrangement and confer increased arsenical resistance to Escherichia coli. Appl. Environ. Microbiol. 66:1826-1833.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1826-1833
    • Butcher, B.G.1    Deane, S.M.2    Rawlings, D.R.E.3
  • 7
    • 0023038352 scopus 로고
    • Nucleotide sequence of the structural gene of an anion pump. The plasmid-encoded arsenical resistance operon
    • Chen, C.-M., T. K. Misra, S. Silver, and B. P. Rosen. 1986. Nucleotide sequence of the structural gene of an anion pump. The plasmid-encoded arsenical resistance operon. J. Biol. Chem. 261:15030-15038.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15030-15038
    • Chen, C.-M.1    Misra, T.K.2    Silver, S.3    Rosen, B.P.4
  • 10
    • 0028363734 scopus 로고
    • Kinetic and site-directed mutagenesis studies of the cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatase
    • Davis, J. P., M.-M. Zhou, and R. L. Van Etten. 1994. Kinetic and site-directed mutagenesis studies of the cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatase. J. Biol. Chem. 269:8734-8740.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8734-8740
    • Davis, J.P.1    Zhou, M.-M.2    Van Etten, R.L.3
  • 11
    • 0028918571 scopus 로고
    • An Escherichia coli chromosomal ars operon homolog is functional in arsenic detoxification and is conserved in gram-negative bacteria
    • Diorio, C., J. Cai, J. Marmor, R. Shinder, and M. S. DuBow. 1995. An Escherichia coli chromosomal ars operon homolog is functional in arsenic detoxification and is conserved in gram-negative bacteria. J. Bacteriol. 177: 2050-2056.
    • (1995) J. Bacteriol. , vol.177 , pp. 2050-2056
    • Diorio, C.1    Cai, J.2    Marmor, J.3    Shinder, R.4    DuBow, M.S.5
  • 12
  • 13
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks, G., T. L. Steck, and D. F. H. Wallace. 1971. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606-2617.
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallace, D.F.H.3
  • 15
    • 0028289612 scopus 로고
    • Properties of the arsenate reductase of plasmid R773
    • Gladysheva, T. B., K. L. Oden, and B. P. Rosen. 1994. Properties of the arsenate reductase of plasmid R773. Biochemistry 33:7288-7293.
    • (1994) Biochemistry , vol.33 , pp. 7288-7293
    • Gladysheva, T.B.1    Oden, K.L.2    Rosen, B.P.3
  • 16
    • 0032079985 scopus 로고    scopus 로고
    • Functional characterization of the low-molecular-mass phosphotyrosine-protein phosphatase of Acinetobacter johnsonii
    • Grangreasse, C., P. Doublet, C. Vincent, E. Vaganay, M. Riberty, B. Duclos, and A. J. Cozzone. 1998. Functional characterization of the low-molecular-mass phosphotyrosine-protein phosphatase of Acinetobacter johnsonii. J. Mol. Biol. 278:339-347.
    • (1998) J. Mol. Biol. , vol.278 , pp. 339-347
    • Grangreasse, C.1    Doublet, P.2    Vincent, C.3    Vaganay, E.4    Riberty, M.5    Duclos, B.6    Cozzone, A.J.7
  • 17
    • 0022486232 scopus 로고
    • Cloning and expression of the glutaredoxin (grx) gene of Escherichia coli
    • Hoog, J.-O., H. von Bahr-Lindstrom, H. Jornvil, and A. Holmgren. 1986. Cloning and expression of the glutaredoxin (grx) gene of Escherichia coli. Gene 43:13-21.
    • (1986) Gene , vol.43 , pp. 13-21
    • Hoog, J.-O.1    Von Bahr-Lindstrom, H.2    Jornvil, H.3    Holmgren, A.4
  • 18
    • 0035413604 scopus 로고    scopus 로고
    • Molecular reactions of protein phosphatases-insights from structure and chemistry
    • Jackson, M. D., and J. M. Denu. 2001. Molecular reactions of protein phosphatases-insights from structure and chemistry. Chem. Rev. 101:2313-2340.
    • (2001) Chem. Rev. , vol.101 , pp. 2313-2340
    • Jackson, M.D.1    Denu, J.M.2
  • 20
    • 0026747877 scopus 로고
    • Regulation and expression of the arsenic resistance operon from Staphylococcus aureus plasmid pI258
    • Ji, G., and S. Silver. 1992. Regulation and expression of the arsenic resistance operon from Staphylococcus aureus plasmid pI258. J. Bacteriol. 174: 3684-3694.
    • (1992) J. Bacteriol. , vol.174 , pp. 3684-3694
    • Ji, G.1    Silver, S.2
  • 21
    • 0026640112 scopus 로고
    • Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258
    • Ji, G., and S. Silver. 1992. Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258. Proc. Natl. Acad. Sci. USA 89:9474-9478.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9474-9478
    • Ji, G.1    Silver, S.2
  • 23
    • 0033806882 scopus 로고    scopus 로고
    • Cloning and characterization of secretory tyrosine phosphatases from Mycobacterium tuberculosis
    • Koul, A., A. Choidas, M. Treder, A. K. Tyagi, K. Drlica, Y. Singh, and A. Ullrich. 2000. Cloning and characterization of secretory tyrosine phosphatases from Mycobacterium tuberculosis. J. Bacteriol. 182:5425-5432.
    • (2000) J. Bacteriol. , vol.182 , pp. 5425-5432
    • Koul, A.1    Choidas, A.2    Treder, M.3    Tyagi, A.K.4    Drlica, K.5    Singh, Y.6    Ullrich, A.7
  • 24
    • 0032145466 scopus 로고    scopus 로고
    • Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis
    • Krafft, T., and J. M. Macy. 1998. Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis. Eur. J. Biochem. 255:647-653.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 647-653
    • Krafft, T.1    Macy, J.M.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0034840634 scopus 로고    scopus 로고
    • Isolates identifiable as Athrospira maxima and Athrospira fusiformis (Oscillatoriales, Cyanobacteria) appear identical on the basis of a morphological study in culture and 16S rRNA sequences
    • Li, R., H. J. Debella, and W. W. Carmichael. 2001. Isolates identifiable as Athrospira maxima and Athrospira fusiformis (Oscillatoriales, Cyanobacteria) appear identical on the basis of a morphological study in culture and 16S rRNA sequences. Phycologia 40:367-371.
    • (2001) Phycologia , vol.40 , pp. 367-371
    • Li, R.1    Debella, H.J.2    Carmichael, W.W.3
  • 27
    • 0030045016 scopus 로고    scopus 로고
    • Cloning, purification, and properties of a phosphotyrosine protein phosphatase from Streptomyces coelicolor A3(2)
    • Li, Y., and W. R. Strohl. 1996. Cloning, purification, and properties of a phosphotyrosine protein phosphatase from Streptomyces coelicolor A3(2). J. Bacteriol. 178:136-142.
    • (1996) J. Bacteriol. , vol.178 , pp. 136-142
    • Li, Y.1    Strohl, W.R.2
  • 28
    • 0028824723 scopus 로고
    • Identification of an essential cysteine residue in the ArsC arsenate reductase of plasmid R773
    • Liu, J., T. B. Gladysheva, L. Lee, and B. P. Rosen. 1995. Identification of an essential cysteine residue in the ArsC arsenate reductase of plasmid R773. Biochemistry 34:13472-13476.
    • (1995) Biochemistry , vol.34 , pp. 13472-13476
    • Liu, J.1    Gladysheva, T.B.2    Lee, L.3    Rosen, B.P.4
  • 29
    • 0030824252 scopus 로고    scopus 로고
    • Ligand interactions of the ArsC arsenate reductase
    • Liu, J., and B. P. Rosen. 1997. Ligand interactions of the ArsC arsenate reductase. J. Biol. Chem. 272:21084-21089.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21084-21089
    • Liu, J.1    Rosen, B.P.2
  • 30
    • 0029817513 scopus 로고    scopus 로고
    • Chrysiogenes arsenatis gen. nov., sp. nov., a new arsenate-respiring bacterium isolated from gold mine wastewater
    • Macy, J. M., K. Nunan, K. D. Hagen, D. R. Dixon, P. J. Harbour, M. Cahill, and L. I. Sly. 1996. Chrysiogenes arsenatis gen. nov., sp. nov., a new arsenate-respiring bacterium isolated from gold mine wastewater. Int. J. Syst. Bacteriol. 46:1153-1157.
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 1153-1157
    • Macy, J.M.1    Nunan, K.2    Hagen, K.D.3    Dixon, D.R.4    Harbour, P.J.5    Cahill, M.6    Sly, L.I.7
  • 31
    • 0035190119 scopus 로고    scopus 로고
    • Insights into the structure, solvation, and mechanism of the ArsC arsenate reductase, a novel arsenic detoxification enzyme
    • Martin, P., S. DeMel, J. Shi, T. Gladysheva, D. L. Gatti, B. P. Rosen, and B. F. P. Edwards. 2001. Insights into the structure, solvation, and mechanism of the ArsC arsenate reductase, a novel arsenic detoxification enzyme. Structure 9:1071-1081.
    • (2001) Structure , vol.9 , pp. 1071-1081
    • Martin, P.1    DeMel, S.2    Shi, J.3    Gladysheva, T.4    Gatti, D.L.5    Rosen, B.P.6    Edwards, B.F.P.7
  • 32
    • 0033592956 scopus 로고    scopus 로고
    • The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus
    • Messens, J., G. Hayburn, A. Desmyter, G. Laus, and L. Wyns. 1999. The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus. Biochemistry 38:16857-16865.
    • (1999) Biochemistry , vol.38 , pp. 16857-16865
    • Messens, J.1    Hayburn, G.2    Desmyter, A.3    Laus, G.4    Wyns, L.5
  • 35
    • 0033953735 scopus 로고    scopus 로고
    • The Drsophila primo locus encodes two low-molecular-weight tyrosine phosphatases
    • Miller, D. T., R. Read, J. Rusconi, and R. L. Cagan. 2000. The Drsophila primo locus encodes two low-molecular-weight tyrosine phosphatases. Gene 243:109.
    • (2000) Gene , vol.243 , pp. 109
    • Miller, D.T.1    Read, R.2    Rusconi, J.3    Cagan, R.L.4
  • 36
    • 0035860779 scopus 로고    scopus 로고
    • 5R motif is required for catalytic activity of Saccharomyces cerevisiae Acr2p arsenate reductase
    • 5R motif is required for catalytic activity of Saccharomyces cerevisiae Acr2p arsenate reductase. J. Biol. Chem. 276:34738-34742.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34738-34742
    • Mukhopadhyay, R.1    Rosen, B.P.2
  • 38
    • 0034647748 scopus 로고    scopus 로고
    • Purification and characterization of Acr2p, the Saccharomyces cerevisiae arsenate reductase
    • Mukhopadhyay, R., J. Shi, and B. P. Rosen. 2000. Purification and characterization of Acr2p, the Saccharomyces cerevisiae arsenate reductase. J. Biol. Chem. 275:21149-21157.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21149-21157
    • Mukhopadhyay, R.1    Shi, J.2    Rosen, B.P.3
  • 39
    • 0031016475 scopus 로고    scopus 로고
    • Virulence and arsenate resistance in yersiniae
    • Neyt, C., M. Iriarte, V. H. Thi, and G. R. Cornelis. 1997. Virulence and arsenate resistance in yersiniae. J. Bacteriol. 179:612-619.
    • (1997) J. Bacteriol. , vol.179 , pp. 612-619
    • Neyt, C.1    Iriarte, M.2    Thi, V.H.3    Cornelis, G.R.4
  • 40
    • 0033629383 scopus 로고    scopus 로고
    • Cell cycle regulation by the Cdc25 phosphatase family
    • Nilsson, I., and I. Hoffmann. 2000. Cell cycle regulation by the Cdc25 phosphatase family. Prog. Cell. Cycle Res. 4:107-114.
    • (2000) Prog. Cell. Cycle Res. , vol.4 , pp. 107-114
    • Nilsson, I.1    Hoffmann, I.2
  • 41
    • 0027520785 scopus 로고
    • A protein-tyrosine/serine phosphatase encoded by the genome of the cyanobacterium Nostoc commune UTEX 584
    • Potts, M., H. Sun, K. Mockaitis, P. J. Kennelly, D. Reed, and N. K. Tonks. 1993. A protein-tyrosine/serine phosphatase encoded by the genome of the cyanobacterium Nostoc commune UTEX 584. J. Biol. Chem. 268:7632-7635.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7632-7635
    • Potts, M.1    Sun, H.2    Mockaitis, K.3    Kennelly, P.J.4    Reed, D.5    Tonks, N.K.6
  • 42
    • 0030999706 scopus 로고    scopus 로고
    • r phosphotyrosine protein phosphatases. Evidence of a long evolutionary history
    • r phosphotyrosine protein phosphatases. Evidence of a long evolutionary history. Int. J. Biochem. Cell Biol. 29:279-292.
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 279-292
    • Ramponi, G.1    Stefani, M.2
  • 43
    • 0018409915 scopus 로고
    • Genetic assignments, strain histories, and properties of pure cultures of cyanobacteria
    • Rippka, R., J. Deruelles, J. B. Waterbury, M. Herdman, and R. Y. Stanier. 1979. Genetic assignments, strain histories, and properties of pure cultures of cyanobacteria. J. Gen. Microbiol. 111:1-61.
    • (1979) J. Gen. Microbiol. , vol.111 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3    Herdman, M.4    Stanier, R.Y.5
  • 44
    • 0037010116 scopus 로고    scopus 로고
    • Biochemistry of arsenic detoxification
    • Rosen, B. P. 2002. Biochemistry of arsenic detoxification. FEBS Lett. 529: 86-92.
    • (2002) FEBS Lett. , vol.529 , pp. 86-92
    • Rosen, B.P.1
  • 45
    • 0017521785 scopus 로고
    • Two systems for the uptake of phosphate in Escherichia coli
    • Rosenberg, H., R. G. Gerdes, and K. Chegwidden. 1977. Two systems for the uptake of phosphate in Escherichia coli. J. Bacteriol. 131:505-511.
    • (1977) J. Bacteriol. , vol.131 , pp. 505-511
    • Rosenberg, H.1    Gerdes, R.G.2    Chegwidden, K.3
  • 46
    • 0026642193 scopus 로고
    • Expression and regulation of the antomite, arsenite, and arsenate resistance operon of Staphylcoccus xylosus plasmid pSX267
    • Rosenstein, R., A. Peschel, B. Wieland, and F. Gotz. 1992. Expression and regulation of the antomite, arsenite, and arsenate resistance operon of Staphylcoccus xylosus plasmid pSX267. J. Bacteriol. 174:3676-3683.
    • (1992) J. Bacteriol. , vol.174 , pp. 3676-3683
    • Rosenstein, R.1    Peschel, A.2    Wieland, B.3    Gotz, F.4
  • 47
    • 0036557991 scopus 로고    scopus 로고
    • Arsenical resistance in the IncHI2 plasmids
    • Ryan, D., and E. Colleran. 2002. Arsenical resistance in the IncHI2 plasmids. Plasmid 47:234-240.
    • (2002) Plasmid , vol.47 , pp. 234-240
    • Ryan, D.1    Colleran, E.2
  • 48
    • 0031764045 scopus 로고    scopus 로고
    • The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: A family portrait
    • Shi, L., M. Potts, and P. J. Kennelly. 1998. The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: a family portrait. FEMS Microbiol. Rev. 22:229-253.
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 229-253
    • Shi, L.1    Potts, M.2    Kennelly, P.J.3
  • 49
    • 0033579499 scopus 로고    scopus 로고
    • Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-mediated arsenate reduction
    • Shi, J., A. Vlamis-Gardikas, F. Aslund, A. Holmgren, and B. P. Rosen. 1999. Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-mediated arsenate reduction. J. Biol. Chem. 274:36039-36042.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36039-36042
    • Shi, J.1    Vlamis-Gardikas, A.2    Aslund, F.3    Holmgren, A.4    Rosen, B.P.5
  • 50
  • 51
    • 0031913712 scopus 로고    scopus 로고
    • Expression and regulation of the arsenic resistance operon of Acidophilium multivorum AIU 301 plasmid pKW301 in Escherichia coli
    • Suzuki, K., N. Wakao, T. Kimura, K. Sakka, and K. Ohmiya. 1998. Expression and regulation of the arsenic resistance operon of Acidophilium multivorum AIU 301 plasmid pKW301 in Escherichia coli. Appl. Environ. Microbiol. 64:411-418.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 411-418
    • Suzuki, K.1    Wakao, N.2    Kimura, T.3    Sakka, K.4    Ohmiya, K.5
  • 52
    • 0028916087 scopus 로고
    • Complete nucleotide sequence of a skin element excised by DNA rearrangement during sporulation in Bacillus subtilis
    • Takemaru, K.-I., M. Mizuno, T. Sato, M. Takeuchi, and Y. Kobayashi. 1995. Complete nucleotide sequence of a skin element excised by DNA rearrangement during sporulation in Bacillus subtilis. Microbiology 141:323-327.
    • (1995) Microbiology , vol.141 , pp. 323-327
    • Takemaru, K.-I.1    Mizuno, M.2    Sato, T.3    Takeuchi, M.4    Kobayashi, Y.5
  • 53
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity and progressive multiple sequence weighting, position specific gap penalties, and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity and progressive multiple sequence weighting, position specific gap penalties, and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 54
    • 0033038516 scopus 로고    scopus 로고
    • Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a protein-tyrosine phosphatase, Wzb
    • Vincent, C., P. Doublet, C. Gangreasse, E. Vaganay, A. J. Cozzone, and B. Duclos. 1999. Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a protein-tyrosine phosphatase, Wzb. J. Bacteriol. 181:3472-3477.
    • (1999) J. Bacteriol. , vol.181 , pp. 3472-3477
    • Vincent, C.1    Doublet, P.2    Gangreasse, C.3    Vaganay, E.4    Cozzone, A.J.5    Duclos, B.6
  • 55
    • 0026528237 scopus 로고
    • Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart
    • Wo, Y.-Y. P., M.-M. Zhou, P. Stevis, J. P. Davis, Z.-Y. Zhang, and R. L. Van Etten. 1992. Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart. Biochemistry 31:1712-1721.
    • (1992) Biochemistry , vol.31 , pp. 1712-1721
    • Wo, Y.-Y.P.1    Zhou, M.-M.2    Stevis, P.3    Davis, J.P.4    Zhang, Z.-Y.5    Van Etten, R.L.6
  • 56
    • 0034815030 scopus 로고    scopus 로고
    • Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty
    • Zegers, I., J. C. Martins, R. Willem, L. Wyns, and J. Messens. 2001. Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty. Nat. Struct. Biol. 8:843-847.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 843-847
    • Zegers, I.1    Martins, J.C.2    Willem, R.3    Wyns, L.4    Messens, J.5
  • 57
    • 0031893253 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: Biological function, structural characteristics, and mechanisms of catalysis
    • Zhang, Z.-Y. 1998. Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanisms of catalysis. Crit. Rev. Biochem. Mol. Biol. 33:1-52.
    • (1998) Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 1-52
    • Zhang, Z.-Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.