메뉴 건너뛰기




Volumn 274, Issue 3, 2007, Pages 805-814

Geranylgeranyl reductase involved in the biosynthesis of archaeal membrane lipids in the hyperthermophilic archaeon Archaeoglobus fulgidus

Author keywords

Archaea; Geranylgeranyl reductase; Isoprenoid; Lipid; Oxidoreductase

Indexed keywords

2,3 DI O GERANYLGERANYLGLYCERYL PHOSPHATE; 2,3 DI O PHYTANYLGLYCERYL PHOSPHATE; 3 O GERANYLGERANYLGLYCERYL PHOSPHATE; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; GERANYLGERANYL PYROPHOSPHATE; GERANYLGERANYL REDUCTASE; GLYCEROL DERIVATIVE; MEMBRANE LIPID; MENAQUINONE; PRENYL REDUCTASE; QUINONE DERIVATIVE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SODIUM DITHIONITE; UNCLASSIFIED DRUG;

EID: 33846424568     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05625.x     Document Type: Article
Times cited : (28)

References (33)
  • 1
    • 0024259139 scopus 로고
    • The lipids of archaebacteria
    • De Rosa M & Gambacorta A (1988) The lipids of archaebacteria. Prog Lipid Res 27, 153-175.
    • (1988) Prog Lipid Res , vol.27 , pp. 153-175
    • De Rosa, M.1    Gambacorta, A.2
  • 3
    • 28244438390 scopus 로고    scopus 로고
    • Recent advances in structural research on ether lipids from archaea including comparative and physiological aspects
    • Koga Y & Morii H (2005) Recent advances in structural research on ether lipids from archaea including comparative and physiological aspects. Biosci Biotechnol Biochem 69, 2019-2034.
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 2019-2034
    • Koga, Y.1    Morii, H.2
  • 4
    • 0029068254 scopus 로고
    • sn-Glycerol-1-phosphate dehydrogenase in Methanobacterium thermoautotrophicum: Key enzyme in biosynthesis of the enantiomeric glycerophosphate backbone of ether phospholipids of archaebacteria
    • Nishihara M & Koga Y (1995) sn-Glycerol-1-phosphate dehydrogenase in Methanobacterium thermoautotrophicum: key enzyme in biosynthesis of the enantiomeric glycerophosphate backbone of ether phospholipids of archaebacteria. J Biochem (Tokyo) 117, 933-935.
    • (1995) J Biochem (Tokyo) , vol.117 , pp. 933-935
    • Nishihara, M.1    Koga, Y.2
  • 5
    • 0030860981 scopus 로고    scopus 로고
    • Purification and properties of sn-glycerol-1-phosphate dehydrogenase from Methanobacterium thermoautotrophicum: Characterization of the biosynthetic enzyme for the enantiomeric glycerophosphate backbone of ether polar lipids of archaea
    • Nishihara M & Koga Y (1997) Purification and properties of sn-glycerol-1-phosphate dehydrogenase from Methanobacterium thermoautotrophicum: characterization of the biosynthetic enzyme for the enantiomeric glycerophosphate backbone of ether polar lipids of archaea. J Biochem (Tokyo) 122, 572-576.
    • (1997) J Biochem (Tokyo) , vol.122 , pp. 572-576
    • Nishihara, M.1    Koga, Y.2
  • 6
    • 0028090148 scopus 로고
    • Isolation and characterization of idsA: The gene for the short chain isoprenyl diphosphate synthase from Methanobacterium thermoautotrophicum
    • Chen A & Poulter CD (1994) Isolation and characterization of idsA: the gene for the short chain isoprenyl diphosphate synthase from Methanobacterium thermoautotrophicum. Arch Biochem Biophys 314, 399-404.
    • (1994) Arch Biochem Biophys , vol.314 , pp. 399-404
    • Chen, A.1    Poulter, C.D.2
  • 7
    • 0028283930 scopus 로고
    • Archaebacterial ether-linked lipid biosynthetic gene. Expression cloning, sequencing, and characterization of geranylgeranyl-diphosphate synthase
    • Ohnuma S-i, Suzuki M & Nishino T (1994) Archaebacterial ether-linked lipid biosynthetic gene. Expression cloning, sequencing, and characterization of geranylgeranyl-diphosphate synthase. J Biol Chem 269, 14792-14797.
    • (1994) J Biol Chem , vol.269 , pp. 14792-14797
    • Ohnuma, S.-I.1    Suzuki, M.2    Nishino, T.3
  • 8
    • 0028209988 scopus 로고
    • A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon
    • Tachibana A (1994) A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis. FEBS Lett 341, 291-294.
    • (1994) Natronobacterium pharaonis. FEBS Lett , vol.341 , pp. 291-294
    • Tachibana, A.1
  • 9
    • 0033979844 scopus 로고    scopus 로고
    • Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecular evolution with alteration in product specificity
    • Tachibana A, Yano Y, Otani S, Nomura N, Sako Y & Taniguchi M (2000) Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecular evolution with alteration in product specificity. Eur J Biochem 267, 321-328.
    • (2000) Eur J Biochem , vol.267 , pp. 321-328
    • Tachibana, A.1    Yano, Y.2    Otani, S.3    Nomura, N.4    Sako, Y.5    Taniguchi, M.6
  • 10
    • 0027486805 scopus 로고    scopus 로고
    • Chen A, Zhang D & Poulter CD (1993) (S)-Geranylgeranylglyceryl phosphate synthase. Purification and characterization of the first pathway-specific enzyme in archaebacterial membrane lipid biosynthesis. J Biol Chem 268, 21701-21705.
    • Chen A, Zhang D & Poulter CD (1993) (S)-Geranylgeranylglyceryl phosphate synthase. Purification and characterization of the first pathway-specific enzyme in archaebacterial membrane lipid biosynthesis. J Biol Chem 268, 21701-21705.
  • 11
    • 0035846527 scopus 로고    scopus 로고
    • Geranylgeranylglyceryl phosphate synthase. Characterization of the recombinant enzyme from Methanobacterium thermoautotrophicum
    • Soderberg T, Chen A & Poulter CD (2001) Geranylgeranylglyceryl phosphate synthase. Characterization of the recombinant enzyme from Methanobacterium thermoautotrophicum. Biochemistry 40, 14847-14854.
    • (2001) Biochemistry , vol.40 , pp. 14847-14854
    • Soderberg, T.1    Chen, A.2    Poulter, C.D.3
  • 12
    • 0038647459 scopus 로고    scopus 로고
    • Purification and characterization of geranylgeranylglyceryl phosphate synthase from a thermoacidophilic archaeon
    • Nemoto N, Oshima T & Yamagishi A (2003) Purification and characterization of geranylgeranylglyceryl phosphate synthase from a thermoacidophilic archaeon, Thermoplasma acidophilum. J Biochem (Tokyo) 133, 651-657.
    • (2003) Thermoplasma acidophilum. J Biochem (Tokyo) , vol.133 , pp. 651-657
    • Nemoto, N.1    Oshima, T.2    Yamagishi, A.3
  • 13
    • 9644264034 scopus 로고    scopus 로고
    • (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids
    • Hemmi H, Shibuya K, Takahashi Y, Nakayama T & Nishino T (2004) (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids. J Biol Chem 279, 50197-50203.
    • (2004) J Biol Chem , vol.279 , pp. 50197-50203
    • Hemmi, H.1    Shibuya, K.2    Takahashi, Y.3    Nakayama, T.4    Nishino, T.5
  • 14
    • 33244479867 scopus 로고    scopus 로고
    • A study of archaeal enzymes involved in polar lipid synthesis linking amino acid sequence information, genomic contexts and lipid composition
    • Daiyasu H, Kuma K, Yokoi T, Morii H, Koga Y & Toh H (2005) A study of archaeal enzymes involved in polar lipid synthesis linking amino acid sequence information, genomic contexts and lipid composition. Archaea 1, 399-410.
    • (2005) Archaea , vol.1 , pp. 399-410
    • Daiyasu, H.1    Kuma, K.2    Yokoi, T.3    Morii, H.4    Koga, Y.5    Toh, H.6
  • 15
    • 0036175119 scopus 로고    scopus 로고
    • Effects of a squalene epoxidase inhibitor, terbinafine, on ether lipid biosyntheses in a thermoacidophilic archaeon
    • Kon T, Nemoto N, Oshima T & Yamagishi A (2002) Effects of a squalene epoxidase inhibitor, terbinafine, on ether lipid biosyntheses in a thermoacidophilic archaeon, Thermoplasma acidophilum. J Bacteriol 184, 1395-1401.
    • (2002) Thermoplasma acidophilum. J Bacteriol , vol.184 , pp. 1395-1401
    • Kon, T.1    Nemoto, N.2    Oshima, T.3    Yamagishi, A.4
  • 16
    • 0034711214 scopus 로고    scopus 로고
    • Morii H, Nishihara M & Koga Y (2000) CTP: 2,3-di-O- geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J Biol Chem 275, 36568-36574.
    • Morii H, Nishihara M & Koga Y (2000) CTP: 2,3-di-O- geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J Biol Chem 275, 36568-36574.
  • 17
    • 0037315018 scopus 로고    scopus 로고
    • CDP-2,3-Di-O-geranylgeranyl-sn- glycerol: 1-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus
    • Morii H & Koga Y (2003) CDP-2,3-Di-O-geranylgeranyl-sn- glycerol: 1-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus. J Bacteriol 185, 1181-1189.
    • (2003) J Bacteriol , vol.185 , pp. 1181-1189
    • Morii, H.1    Koga, Y.2
  • 18
    • 10044290651 scopus 로고    scopus 로고
    • Cold adaptation in the antarctic archaeon Methanococcoides burtonii involves membrane lipid unsaturation
    • Nichols DS, Miller MR, Davies NW, Goodchild A, Raftery M & Cavicchioli R (2004) Cold adaptation in the antarctic archaeon Methanococcoides burtonii involves membrane lipid unsaturation. J Bacteriol 186, 8508-8515.
    • (2004) J Bacteriol , vol.186 , pp. 8508-8515
    • Nichols, D.S.1    Miller, M.R.2    Davies, N.W.3    Goodchild, A.4    Raftery, M.5    Cavicchioli, R.6
  • 20
    • 0019490792 scopus 로고
    • Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication
    • Collins MD & Jones D (1981) Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication. Microbiol Rev 45, 316-354.
    • (1981) Microbiol Rev , vol.45 , pp. 316-354
    • Collins, M.D.1    Jones, D.2
  • 21
    • 14644401708 scopus 로고    scopus 로고
    • Menaquinone-specific prenyl reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus
    • Hemmi H, Takahashi Y, Shibuya K, Nakayama T & Nishino T (2005) Menaquinone-specific prenyl reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus. J Bacteriol 187, 1937-1944.
    • (2005) J Bacteriol , vol.187 , pp. 1937-1944
    • Hemmi, H.1    Takahashi, Y.2    Shibuya, K.3    Nakayama, T.4    Nishino, T.5
  • 22
    • 0032518315 scopus 로고    scopus 로고
    • Metabolic compartmentation of plastid prenyllipid biosynthesis - evidence for the involvement of a multifunctional geranylgeranyl reductase
    • Keller Y, Bouvier F, d'Harlingue A & Camara B (1998) Metabolic compartmentation of plastid prenyllipid biosynthesis - evidence for the involvement of a multifunctional geranylgeranyl reductase. Eur J Biochem 251, 413-417.
    • (1998) Eur J Biochem , vol.251 , pp. 413-417
    • Keller, Y.1    Bouvier, F.2    d'Harlingue, A.3    Camara, B.4
  • 23
    • 0032818240 scopus 로고    scopus 로고
    • Reduced activity of geranylgeranyl reductase leads to loss of chlorophyll and tocopherol and to partially geranylgeranylated chlorophyll in transgenic tobacco plants expressing antisense RNA for geranylgeranyl reductase
    • Tanaka R, Oster U, Kruse E, Rudiger W & Grimm B (1999) Reduced activity of geranylgeranyl reductase leads to loss of chlorophyll and tocopherol and to partially geranylgeranylated chlorophyll in transgenic tobacco plants expressing antisense RNA for geranylgeranyl reductase. Plant Physiol 120, 695-704.
    • (1999) Plant Physiol , vol.120 , pp. 695-704
    • Tanaka, R.1    Oster, U.2    Kruse, E.3    Rudiger, W.4    Grimm, B.5
  • 24
    • 0030199898 scopus 로고    scopus 로고
    • Cloning, sequencing and functional assignment of the chlorophyll biosynthesis gene, chlP, of Synechocystis sp. PCC 6803
    • Addlesee HA, Gibson LC, Jensen PE & Hunter CN (1996) Cloning, sequencing and functional assignment of the chlorophyll biosynthesis gene, chlP, of Synechocystis sp. PCC 6803. FEBS Lett 389, 126-130.
    • (1996) FEBS Lett , vol.389 , pp. 126-130
    • Addlesee, H.A.1    Gibson, L.C.2    Jensen, P.E.3    Hunter, C.N.4
  • 25
    • 0026649367 scopus 로고
    • Gas chromatographic determination of isoprenoid alkylglycerol diethers in archaebacterial cultures and environmental samples
    • Teixidor P & Grimalt JO (1992) Gas chromatographic determination of isoprenoid alkylglycerol diethers in archaebacterial cultures and environmental samples. J Chromatogr A 607, 253-259.
    • (1992) J Chromatogr A , vol.607 , pp. 253-259
    • Teixidor, P.1    Grimalt, J.O.2
  • 26
    • 33746899029 scopus 로고    scopus 로고
    • Biosynthesis of archaeal membrane lipids: Digeranylgeranylglycerophospholipid reductase of the thermoacidophilic archaeon Thermoplasma acidophilum
    • Nishimura Y & Eguchi T (2006) Biosynthesis of archaeal membrane lipids: digeranylgeranylglycerophospholipid reductase of the thermoacidophilic archaeon Thermoplasma acidophilum. J Biochem (Tokyo) 139, 1073-1081.
    • (2006) J Biochem (Tokyo) , vol.139 , pp. 1073-1081
    • Nishimura, Y.1    Eguchi, T.2
  • 27
    • 0035999985 scopus 로고    scopus 로고
    • Amphiphilicity index of polar amino acids as an aid in the characterization of amino acid preference at membrane-water interfaces
    • Mitaku S, Hirokawa T & Tsuji T (2002) Amphiphilicity index of polar amino acids as an aid in the characterization of amino acid preference at membrane-water interfaces. Bioinformatics 18, 608-616.
    • (2002) Bioinformatics , vol.18 , pp. 608-616
    • Mitaku, S.1    Hirokawa, T.2    Tsuji, T.3
  • 29
    • 0000171230 scopus 로고
    • A new method for preparing flavinadenine dinucleotide
    • Whitby LG (1953) A new method for preparing flavinadenine dinucleotide. Biochem J 54, 437-442.
    • (1953) Biochem J , vol.54 , pp. 437-442
    • Whitby, L.G.1
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive 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
  • 31
    • 0020482354 scopus 로고
    • Efficient enzymatic hydrolysis of polyprenyl pyrophosphates
    • Fujii H, Koyama T & Ogura K (1982) Efficient enzymatic hydrolysis of polyprenyl pyrophosphates. Biochim Biophys Acta 712, 716-718.
    • (1982) Biochim Biophys Acta , vol.712 , pp. 716-718
    • Fujii, H.1    Koyama, T.2    Ogura, K.3
  • 32
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG & Dyer WJ (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37, 911-917.
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 33
    • 0026528419 scopus 로고
    • Quantitative determination of methanogenic cells based on analysis of ether-linked glycerolipids by high-performance liquid chromatography
    • Demizu K, Ohtsubo S, Kohno S, Miura I, Nishihara M & Koga Y (1992) Quantitative determination of methanogenic cells based on analysis of ether-linked glycerolipids by high-performance liquid chromatography. J Ferment Bioeng 73, 135-139.
    • (1992) J Ferment Bioeng , vol.73 , pp. 135-139
    • Demizu, K.1    Ohtsubo, S.2    Kohno, S.3    Miura, I.4    Nishihara, M.5    Koga, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.