메뉴 건너뛰기




Volumn 6, Issue 3, 2002, Pages 245-251

A new type of dihydroorotate dehydrogenase, type 1S, from the thermoacidophilic archaeon Sulfolobus solfataricus

Author keywords

Characterization; Dihydroorotate dehydrogenase; Purification; Sequence analysis; Sulfolobus solfataricus

Indexed keywords

ARCHAEA; SULFOLOBUS SOLFATARICUS;

EID: 18744363004     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-001-0249-0     Document Type: Article
Times cited : (20)

References (15)
  • 1
    • 0034730083 scopus 로고    scopus 로고
    • Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechanism of catalysis
    • Argyrou A, Washabaugh MW, Pickart CM (2000) Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechanism of catalysis. Biochemistry 39:10373-10384
    • (2000) Biochemistry , vol.39 , pp. 10373-10384
    • Argyrou, A.1    Washabaugh, M.W.2    Pickart, C.M.3
  • 2
    • 0039021706 scopus 로고    scopus 로고
    • The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis
    • Björnberg O, Grüner A-C, Roepstorff P, Jensen KF (1999) The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis. Biochemistry 39:2899-2908
    • (1999) Biochemistry , vol.39 , pp. 2899-2908
    • Björnberg, O.1    Grüner, A.-C.2    Roepstorff, P.3    Jensen, K.F.4
  • 3
    • 0013612812 scopus 로고
    • Steady state kinetics
    • Boyer PD (ed). Academic Press, New York
    • Cleland WW (1971) Steady state kinetics. In: Boyer PD (ed) The enzymes, 3rd edn, vol 2. Academic Press, New York, pp 1-65
    • (1971) The Enzymes, 3rd Edn , vol.2 , pp. 1-65
    • Cleland, W.W.1
  • 4
    • 0023009615 scopus 로고
    • Purification and properties of the bovine liver mitochondrial dihydroorotate dehydrogenase
    • Hines V, Keys LD, Johnston M (1986) Purification and properties of the bovine liver mitochondrial dihydroorotate dehydrogenase. J Biol Chem 261:11386-11392
    • (1986) J Biol Chem , vol.261 , pp. 11386-11392
    • Hines, V.1    Keys, L.D.2    Johnston, M.3
  • 5
    • 0003081753 scopus 로고    scopus 로고
    • Evolutionary and functional families of dihydroorotate dehydrogenases
    • Dept. of Microbiology & Immunology, University of Kentucky, Lexington
    • Jensen KF, Björnberg O (1998) Evolutionary and functional families of dihydroorotate dehydrogenases. In: Paths to pyrimidines, vol 6. Dept. of Microbiology & Immunology, University of Kentucky, Lexington, pp 20-28
    • (1998) Paths to Pyrimidines , vol.6 , pp. 20-28
    • Jensen, K.F.1    Björnberg, O.2
  • 6
    • 0034213171 scopus 로고    scopus 로고
    • Catalytic properties of dihydroorotate dehydrogenase from Saccharomyces cerevisiae: Studies on pH, alternate substrates, and inhibitors
    • Jordan DB, Bisaha JB, Picollelli MA (2000) Catalytic properties of dihydroorotate dehydrogenase from Saccharomyces cerevisiae: studies on pH, alternate substrates, and inhibitors. Arch Biochem Biophys 378:84-92
    • (2000) Arch Biochem Biophys , vol.378 , pp. 84-92
    • Jordan, D.B.1    Bisaha, J.B.2    Picollelli, M.A.3
  • 7
    • 0017795563 scopus 로고
    • Dihydroorotate dehydrogenase (Escherichia coli)
    • Karibian D (1978) Dihydroorotate dehydrogenase (Escherichia coli). Methods Enzymol 51:58-63
    • (1978) Methods Enzymol , vol.51 , pp. 58-63
    • Karibian, D.1
  • 8
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 9
    • 0034650342 scopus 로고    scopus 로고
    • Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents
    • Liu S, Neidhardt EA, Grossmann TH, Ocain T, Clardy J (2000) Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents. Structure 8:25-33
    • (2000) Structure , vol.8 , pp. 25-33
    • Liu, S.1    Neidhardt, E.A.2    Grossmann, T.H.3    Ocain, T.4    Clardy, J.5
  • 10
    • 0017832712 scopus 로고
    • Dihydroorotate dehydrogenase (Neurospora crassa)
    • Miller RW (1978) Dihydroorotate dehydrogenase (Neurospora crassa). Methods Enzymol. 51:63-69
    • (1978) Methods Enzymol , vol.51 , pp. 63-69
    • Miller, R.W.1
  • 11
    • 0029800334 scopus 로고    scopus 로고
    • The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers
    • Nielsen FS, Andersen PS, Jensen KF (1996a) The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers. J Biol Chem 271:29359-29365
    • (1996) J Biol Chem , vol.271 , pp. 29359-29365
    • Nielsen, F.S.1    Andersen, P.S.2    Jensen, K.F.3
  • 12
    • 0029970387 scopus 로고    scopus 로고
    • Purification and characterization of dihydroorotate dehydrogenase a from Lactococcus lactis: Crystallization and preliminary X-ray diffraction studies of the enzyme
    • Nielsen FS, Rowland P, Larsen S, Jensen KF (1996b) Purification and characterization of dihydroorotate dehydrogenase A from Lactococcus lactis: crystallization and preliminary X-ray diffraction studies of the enzyme. Protein Sci 5:852-856
    • (1996) Protein Sci , vol.5 , pp. 852-856
    • Nielsen, F.S.1    Rowland, P.2    Larsen, S.3    Jensen, K.F.4
  • 13
    • 0021755637 scopus 로고
    • Mechanistic studies with deuterated dihydroorotates on the dihydroorotate oxidase from Crithidia fasciculata
    • Pascal RA, Walsh CT (1984) Mechanistic studies with deuterated dihydroorotates on the dihydroorotate oxidase from Crithidia fasciculata. Biochemistry 23:2745-2752
    • (1984) Biochemistry , vol.23 , pp. 2745-2752
    • Pascal, R.A.1    Walsh, C.T.2
  • 14
    • 0010184353 scopus 로고    scopus 로고
    • Structure of dihydroorotate dehydrogenase B: Electron transfer between two flavin groups bridged by an iron-sulphur cluster
    • Rowland P, Nørager S, Jensen KF, Larsen S (2000) Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster. Structure 8:1227-1238
    • (2000) Structure , vol.8 , pp. 1227-1238
    • Rowland, P.1    Nørager, S.2    Jensen, K.F.3    Larsen, S.4
  • 15
    • 27144475130 scopus 로고    scopus 로고
    • Dihydroorotate dehydrogenase from the thermoacidophilic archaeon Sulfolobus solfataricus is a cytosolic dimer
    • Ghisla S, Kroneck P, Macheroux P, Sund H (eds). Weber, Berlin
    • Sørensen PG, Dandanell G (1999) Dihydroorotate dehydrogenase from the thermoacidophilic archaeon Sulfolobus solfataricus is a cytosolic dimer. In: Ghisla S, Kroneck P, Macheroux P, Sund H (eds) Flavins and flavoproteins. Weber, Berlin, pp 619-622
    • (1999) Flavins and Flavoproteins , pp. 619-622
    • Sørensen, P.G.1    Dandanell, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.