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Volumn 1748, Issue 1, 2005, Pages 110-115

The first archaeal agmatinase from anaerobic hyperthermophilic archaeon Pyrococcus horikoshii: Cloning, expression, and characterization

Author keywords

Agmatinase; Agmatine; Archaea; Polyamine; Pyrococcus horikoshii

Indexed keywords

AGMATINE; ARGININE; BACTERIAL ENZYME; CALCIUM ION; COBALT; GUANIDINE; HYDROCHLORIC ACID; MANGANESE; RECOMBINANT AGMATINASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 14744292577     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.12.010     Document Type: Article
Times cited : (18)

References (27)
  • 2
    • 0030098067 scopus 로고    scopus 로고
    • Imidazoline receptors and agmatine in blood vessels: A novel system inhibiting vascular smooth muscle proliferation
    • S. Regunathan, C. Youngson, W. Raasch, H. Wang, and D.J. Reis Imidazoline receptors and agmatine in blood vessels: a novel system inhibiting vascular smooth muscle proliferation J. Pharmacol. Exp. Ther. 276 1996 1272 1282
    • (1996) J. Pharmacol. Exp. Ther. , vol.276 , pp. 1272-1282
    • Regunathan, S.1    Youngson, C.2    Raasch, W.3    Wang, H.4    Reis, D.J.5
  • 3
    • 0032796565 scopus 로고    scopus 로고
    • Anti-proliferative and anti-inflammatory actions of imidazoline agents. Are imidazoline receptors involved?
    • S. Regunathan, D.L. Feinstein, and D.J. Reis Anti-proliferative and anti-inflammatory actions of imidazoline agents. Are imidazoline receptors involved? Ann. N.Y. Acad. Sci. 881 1999 410 419
    • (1999) Ann. N.Y. Acad. Sci. , vol.881 , pp. 410-419
    • Regunathan, S.1    Feinstein, D.L.2    Reis, D.J.3
  • 6
    • 0002304850 scopus 로고
    • Biochemical function of unusual polyamines found in the cells of extreme thermophiles
    • S.H. Goldemberg D. Algranati IRL Press Oxford
    • T. Oshima, N. Hamazaki, T. Uzawa, and S.M. Friedman Biochemical function of unusual polyamines found in the cells of extreme thermophiles S.H. Goldemberg D. Algranati In the biology and chemistry of polyamines 1990 IRL Press Oxford 1 9
    • (1990) In the Biology and Chemistry of Polyamines , pp. 1-9
    • Oshima, T.1    Hamazaki, N.2    Uzawa, T.3    Friedman, S.M.4
  • 8
    • 0026788035 scopus 로고
    • Polyamines as a chemotaxonomic marker in bacterial systematics
    • K. Hamana, and S. Matsuzaki Polyamines as a chemotaxonomic marker in bacterial systematics Crit. Rev. Microbiol. 18 1992 261 283
    • (1992) Crit. Rev. Microbiol. , vol.18 , pp. 261-283
    • Hamana, K.1    Matsuzaki, S.2
  • 9
    • 0033417912 scopus 로고    scopus 로고
    • Polyamines of the thermophilic eubacteria belonging to the genera Aquifex, Thermodesulfobacterium, Thermus and Meiothermus, and the thermophilic archaebacteria belonging to the genera Sulfurisphaera, Sulfophobococcus, Stetteria, Thermocladium, Pyrococcus, Thermococcus, Methanopyrus and Methanothermus
    • K. Hamana, H. Hamana, T. Shinozawa, M. Niitsu, K. Samejima, and T. Itoh Polyamines of the thermophilic eubacteria belonging to the genera Aquifex, Thermodesulfobacterium, Thermus and Meiothermus, and the thermophilic archaebacteria belonging to the genera Sulfurisphaera, Sulfophobococcus, Stetteria, Thermocladium, Pyrococcus, Thermococcus, Methanopyrus and Methanothermus Microbios 97 1999 117 130
    • (1999) Microbios , vol.97 , pp. 117-130
    • Hamana, K.1    Hamana, H.2    Shinozawa, T.3    Niitsu, M.4    Samejima, K.5    Itoh, T.6
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • W.W. Cleland Statistical analysis of enzyme kinetic data Methods Enzymol. 63 1979 103 138
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 14
    • 0020688237 scopus 로고
    • Cloning of the Escherichia coli genes for the biosynthetic enzymes for polyamines
    • C.W. Tabor, H. Tabor, E.W. Hafner, G.D. Markham, and S.M. Boyle Cloning of the Escherichia coli genes for the biosynthetic enzymes for polyamines Methods Enzymol. 94 1983 117 121
    • (1983) Methods Enzymol. , vol.94 , pp. 117-121
    • Tabor, C.W.1    Tabor, H.2    Hafner, E.W.3    Markham, G.D.4    Boyle, S.M.5
  • 15
    • 0042266874 scopus 로고    scopus 로고
    • Molecular cloning of the gene for edeine B1 amidinohydrolase in addition to the agmatinase activity in Bacillus subtilis
    • K.W. Shimotohno, T. Hidaka, T. Morishita, and T. Endo Molecular cloning of the gene for edeine B1 amidinohydrolase in addition to the agmatinase activity in Bacillus subtilis Biol. Pharm. Bull. 26 2003 262 265
    • (2003) Biol. Pharm. Bull. , vol.26 , pp. 262-265
    • Shimotohno, K.W.1    Hidaka, T.2    Morishita, T.3    Endo, T.4
  • 16
    • 0028048859 scopus 로고
    • Cloning, sequencing and disruption of a gene from Streptomyces clavuligerus involved in clavulanic acid biosynthesis
    • K.A. Aidoo, A. Wong, D.C. Alexander, R.A. Rittammer, and S.E. Jensen Cloning, sequencing and disruption of a gene from Streptomyces clavuligerus involved in clavulanic acid biosynthesis Gene 147 1994 41 46
    • (1994) Gene , vol.147 , pp. 41-46
    • Aidoo, K.A.1    Wong, A.2    Alexander, D.C.3    Rittammer, R.A.4    Jensen, S.E.5
  • 18
    • 84987049314 scopus 로고
    • Purification and properties of agmatine amidinohydrolase of Evernia prunastri
    • C. Vicente, and M.E. Legaz Purification and properties of agmatine amidinohydrolase of Evernia prunastri Physiol. Plant. 55 1982 335 339
    • (1982) Physiol. Plant. , vol.55 , pp. 335-339
    • Vicente, C.1    Legaz, M.E.2
  • 19
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 20
    • 0022510568 scopus 로고
    • Purification and properties of agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli
    • C. Satishchandran, and S.M. Boyle Purification and properties of agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli J. Bacteriol. 165 1986 843 848
    • (1986) J. Bacteriol. , vol.165 , pp. 843-848
    • Satishchandran, C.1    Boyle, S.M.2
  • 22
    • 0029789277 scopus 로고
    • Agmatinase activity in rat brain: A metabolic pathway for the degradation of agmatine
    • M. Sastre, S. Regunathan, E. Galea, and D.J. Reis Agmatinase activity in rat brain: a metabolic pathway for the degradation of agmatine J. Neurochem. 67 1995 1761 1765
    • (1995) J. Neurochem. , vol.67 , pp. 1761-1765
    • Sastre, M.1    Regunathan, S.2    Galea, E.3    Reis, D.J.4
  • 24
    • 0014010850 scopus 로고
    • Multiple pathways of putrescine biosynthesis in Escherichia coli
    • D.R. Morris, and A.B. Pardee Multiple pathways of putrescine biosynthesis in Escherichia coli J. Biol. Chem. 241 1966 3129 3135
    • (1966) J. Biol. Chem. , vol.241 , pp. 3129-3135
    • Morris, D.R.1    Pardee, A.B.2
  • 25
    • 0015721317 scopus 로고
    • Purification and some properties of l-arginase from Bacillus subtilis
    • N. Nakamura, M. Fujita, and K. Kimura Purification and some properties of l-arginase from Bacillus subtilis Agric. Biol. Chem. 37 1973 2827 2833
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 2827-2833
    • Nakamura, N.1    Fujita, M.2    Kimura, K.3
  • 27
    • 0033894954 scopus 로고    scopus 로고
    • Phylogeny of related functions: The case of polyamine biosynthetic enzymes
    • A. Sekowska, A. Danchin, and J.L. Risler Phylogeny of related functions: the case of polyamine biosynthetic enzymes Microbiology 146 2000 1815 1828
    • (2000) Microbiology , vol.146 , pp. 1815-1828
    • Sekowska, A.1    Danchin, A.2    Risler, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.