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Volumn 43, Issue 3, 2008, Pages 207-213

Identification and functional expression of a Δ9-fatty acid desaturase from Psychrobacter urativorans in Escherichia coli

Author keywords

9 fatty acid desaturase; Degenerate primer; Fatty acid composition; Gene expression

Indexed keywords

ACYL COENZYME A DESATURASE; DELTA9 FATTY ACID DESATURASE; HISTIDINE; PALMITIC ACID; PALMITOLEIC ACID; UNCLASSIFIED DRUG;

EID: 41149128662     PISSN: 00244201     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11745-007-3150-5     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 1942437999 scopus 로고    scopus 로고
    • Fatty acid desaturases: Selecting the dehydrogenation channel
    • Buist PH (2004) Fatty acid desaturases: selecting the dehydrogenation channel. Nat Prod Rep 21:249-262
    • (2004) Nat Prod Rep , vol.21 , pp. 249-262
    • Buist, P.H.1
  • 2
    • 0031659941 scopus 로고    scopus 로고
    • Structure and expression of fatty acid desaturases
    • Los DA, Murata N (1998) Structure and expression of fatty acid desaturases. Biochim Biophys Acta 1394:3-15
    • (1998) Biochim Biophys Acta , vol.1394 , pp. 3-15
    • Los, D.A.1    Murata, N.2
  • 4
    • 0002361795 scopus 로고
    • Acyl-CoA desaturases and the adaptive regulation of membrane lipid composition
    • Cossins AR ed, Portland Press, London
    • Macartney AI, Maresca B, Cossins AR (1994) Acyl-CoA desaturases and the adaptive regulation of membrane lipid composition. In: Cossins AR (ed) Temperature adaptation of biological membranes. Portland Press, London
    • (1994) Temperature adaptation of biological membranes
    • Macartney, A.I.1    Maresca, B.2    Cossins, A.R.3
  • 5
    • 33749040473 scopus 로고    scopus 로고
    • Mechanisms of temperature adaptation in poikilotherms
    • Guschina IA, Harwood JL (2006) Mechanisms of temperature adaptation in poikilotherms. FEBS Lett 580:5477-5483
    • (2006) FEBS Lett , vol.580 , pp. 5477-5483
    • Guschina, I.A.1    Harwood, J.L.2
  • 8
    • 0028518741 scopus 로고
    • Purification and PCR-based cDNA cloning of a plastidial n-6 desaturase
    • Schmidt H, Dresselhaus T, Buck F, Heinz E (1994) Purification and PCR-based cDNA cloning of a plastidial n-6 desaturase. Plant Mol Biol 26:631-642
    • (1994) Plant Mol Biol , vol.26 , pp. 631-642
    • Schmidt, H.1    Dresselhaus, T.2    Buck, F.3    Heinz, E.4
  • 9
    • 33745299710 scopus 로고    scopus 로고
    • Cloning and molecular characterization of Delta 12-fatty acid desaturase gene from Mortierella isabellina
    • Li MC, Li H, Wei DS, Xing LJ (2006) Cloning and molecular characterization of Delta 12-fatty acid desaturase gene from Mortierella isabellina. World J Gastroenterol 12:3373-3379
    • (2006) World J Gastroenterol , vol.12 , pp. 3373-3379
    • Li, M.C.1    Li, H.2    Wei, D.S.3    Xing, L.J.4
  • 10
    • 0037189913 scopus 로고    scopus 로고
    • A desaturase-like protein from white spruce is a Delta9 desaturase
    • Marillia EF, Giblin EM, Covello PS, Taylor DC (2002) A desaturase-like protein from white spruce is a Delta9 desaturase. FEBS Lett 526:49-52
    • (2002) FEBS Lett , vol.526 , pp. 49-52
    • Marillia, E.F.1    Giblin, E.M.2    Covello, P.S.3    Taylor, D.C.4
  • 11
    • 12444272688 scopus 로고    scopus 로고
    • Mutation study of conserved amino acid residues of Spirulina Delta6 acyl-lipid desaturase showing involvement of histidine 313 in the regioselectivity of the enzyme
    • Hongsthong A, Subudhi S, Sirijuntarat M, Cheevadhanarak S (2004) Mutation study of conserved amino acid residues of Spirulina Delta6 acyl-lipid desaturase showing involvement of histidine 313 in the regioselectivity of the enzyme. Appl Microbiol Biotechnol 66:74-84
    • (2004) Appl Microbiol Biotechnol , vol.66 , pp. 74-84
    • Hongsthong, A.1    Subudhi, S.2    Sirijuntarat, M.3    Cheevadhanarak, S.4
  • 12
    • 29044438514 scopus 로고    scopus 로고
    • Targeted mutagenesis of a fatty acid Delta6 desaturase from Mucor rouxii: Role of amino acid residues adjacent to histidine-rich motif II
    • Na-Ranong S, Laoteng K, Kittakoop P, Tanticharoen M, Cheevadhanarak S (2006) Targeted mutagenesis of a fatty acid Delta6 desaturase from Mucor rouxii: role of amino acid residues adjacent to histidine-rich motif II. Biochem Biophys Res Commun 339:1029-1034
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 1029-1034
    • Na-Ranong, S.1    Laoteng, K.2    Kittakoop, P.3    Tanticharoen, M.4    Cheevadhanarak, S.5
  • 13
    • 0015207608 scopus 로고
    • Alteration in fatty acid chain length in Micrococcus cryophilus grown at different temperatures
    • Russell NJ (1971) Alteration in fatty acid chain length in Micrococcus cryophilus grown at different temperatures. Biochim Biophys Acta 231:254-256
    • (1971) Biochim Biophys Acta , vol.231 , pp. 254-256
    • Russell, N.J.1
  • 14
    • 0017731360 scopus 로고
    • Desaturation of fatty acids by the psychrophilic bacterium Micrococcus cryophilus
    • Russell NJ (1977) Desaturation of fatty acids by the psychrophilic bacterium Micrococcus cryophilus. Biochem Soc Trans 5:1492-1494
    • (1977) Biochem Soc Trans , vol.5 , pp. 1492-1494
    • Russell, N.J.1
  • 15
    • 0018087119 scopus 로고
    • The positional specificity of a desaturase in the psychrophilic bacterium Micrococcus cryophilus (ATCC 15174)
    • Russell NJ (1978) The positional specificity of a desaturase in the psychrophilic bacterium Micrococcus cryophilus (ATCC 15174). Biochim Biophys Acta 531:179-186
    • (1978) Biochim Biophys Acta , vol.531 , pp. 179-186
    • Russell, N.J.1
  • 16
    • 0020664022 scopus 로고
    • Some properties, including the substrate in vivo, of the Delta9-desaturase in Micrococcus cryophilus
    • Foot M, Jeffcoat R, Russell NJ (1983) Some properties, including the substrate in vivo, of the Delta9-desaturase in Micrococcus cryophilus. Biochem J 209:345-353
    • (1983) Biochem J , vol.209 , pp. 345-353
    • Foot, M.1    Jeffcoat, R.2    Russell, N.J.3
  • 18
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 19
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 20
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Moller S, Croning MD, Apweiler R (2001) Evaluation of methods for the prediction of membrane spanning regions. Bioinformatics 17:646-653
    • (2001) Bioinformatics , vol.17 , pp. 646-653
    • Moller, S.1    Croning, M.D.2    Apweiler, R.3
  • 22
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 23
    • 19444384553 scopus 로고    scopus 로고
    • CODEHOP-mediated PCR - a powerful technique for the identification and characterization of viral genomes
    • Rose TM (2005) CODEHOP-mediated PCR - a powerful technique for the identification and characterization of viral genomes. Virol J 2:20
    • (2005) Virol , vol.J 2 , pp. 20
    • Rose, T.M.1
  • 24
    • 0028089687 scopus 로고
    • Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase
    • Shanklin J, Whittle E, Fox BG (1994) Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase. Biochemistry 33:12787-12794
    • (1994) Biochemistry , vol.33 , pp. 12787-12794
    • Shanklin, J.1    Whittle, E.2    Fox, B.G.3
  • 25
    • 0025242338 scopus 로고
    • The OLE1 gene of Saccharomyces cerevisiae encodes the Delta9 fatty acid desaturase and can be functionally replaced by the rat stearoyl-CoA desaturase gene
    • Stukey JE, McDonough VM, Martin CE (1990) The OLE1 gene of Saccharomyces cerevisiae encodes the Delta9 fatty acid desaturase and can be functionally replaced by the rat stearoyl-CoA desaturase gene. J Biol Chem 265:20144-20149
    • (1990) J Biol Chem , vol.265 , pp. 20144-20149
    • Stukey, J.E.1    McDonough, V.M.2    Martin, C.E.3
  • 26
    • 33644861793 scopus 로고    scopus 로고
    • Membrane topology of mouse stearoyl-CoA desaturase 1
    • Man WC, Miyazaki M, Chu K, Ntambi JM (2006) Membrane topology of mouse stearoyl-CoA desaturase 1. J Biol Chem 281:1251-1260
    • (2006) J Biol Chem , vol.281 , pp. 1251-1260
    • Man, W.C.1    Miyazaki, M.2    Chu, K.3    Ntambi, J.M.4
  • 27
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10:1-6
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 28
    • 0031783528 scopus 로고    scopus 로고
    • Overproduction of a functional fatty acid biosynthetic enzyme blocks fatty acid synthesis in Escherichia coli
    • Subrahmanyam S, Cronan JE Jr (1998) Overproduction of a functional fatty acid biosynthetic enzyme blocks fatty acid synthesis in Escherichia coli. J Bacteriol 180:4596-4602
    • (1998) J Bacteriol , vol.180 , pp. 4596-4602
    • Subrahmanyam, S.1    Cronan Jr, J.E.2
  • 29
    • 13344257543 scopus 로고
    • Micrococcus cryophilus, spec. nov.; a large coccus especially suitable for cytologic study
    • McLean LR, Sulzbacher WL, Mudd S (1951) Micrococcus cryophilus, spec. nov.; a large coccus especially suitable for cytologic study. J Bacteriol 62:723-728
    • (1951) J Bacteriol , vol.62 , pp. 723-728
    • McLean, L.R.1    Sulzbacher, W.L.2    Mudd, S.3
  • 30
    • 84983075152 scopus 로고    scopus 로고
    • Delta9 desaturase gene
    • US Patent 6,448,055
    • Shimizu S, Kobayashi M (2002) Delta9 desaturase gene. US Patent 6,448,055
    • (2002)
    • Shimizu, S.1    Kobayashi, M.2
  • 31
    • 0028172108 scopus 로고
    • Delta9 Acyl-lipid desaturases of cyanobacteria. Molecular cloning and substrate specificities in terms of fatty acids, sn-positions, and polar head groups
    • Sakamoto T, Wada H, Nishida I, Ohmori M, Murata N (1994) Delta9 Acyl-lipid desaturases of cyanobacteria. Molecular cloning and substrate specificities in terms of fatty acids, sn-positions, and polar head groups. J Biol Chem 269:25576-25580
    • (1994) J Biol Chem , vol.269 , pp. 25576-25580
    • Sakamoto, T.1    Wada, H.2    Nishida, I.3    Ohmori, M.4    Murata, N.5
  • 33
    • 33748358831 scopus 로고    scopus 로고
    • A novel Delta9 acyl-lipid desaturase, DesC2, from cyanobacteria acts on fatty acids esterified to the sn-2 position of glycerolipids
    • Chintalapati S, Prakash JS, Gupta P, Ohtani S, Suzuki I, Sakamoto T, Murata N, Shivaji S (2006) A novel Delta9 acyl-lipid desaturase, DesC2, from cyanobacteria acts on fatty acids esterified to the sn-2 position of glycerolipids. Biochem J 398:207-214
    • (2006) Biochem J , vol.398 , pp. 207-214
    • Chintalapati, S.1    Prakash, J.S.2    Gupta, P.3    Ohtani, S.4    Suzuki, I.5    Sakamoto, T.6    Murata, N.7    Shivaji, S.8
  • 35
    • 0024424620 scopus 로고
    • Isolation and characterization of OLE1, a gene affecting fatty acid desaturation from Saccharomyces cerevisiae
    • Stukey JE, McDonough VM, Martin CE (1989) Isolation and characterization of OLE1, a gene affecting fatty acid desaturation from Saccharomyces cerevisiae. J Biol Chem 264:16537-16544
    • (1989) J Biol Chem , vol.264 , pp. 16537-16544
    • Stukey, J.E.1    McDonough, V.M.2    Martin, C.E.3
  • 36
    • 0035987262 scopus 로고    scopus 로고
    • A third fatty acid Delta9 desaturase from Mortierella alpina with a different substrate specificity to ole1p and ole2p
    • MacKenzie DA, Carter AT, Wongwathanarat P, Eagles J, Salt J, Archer DB (2002) A third fatty acid Delta9 desaturase from Mortierella alpina with a different substrate specificity to ole1p and ole2p. Microbiology 148:1725-1735
    • (2002) Microbiology , vol.148 , pp. 1725-1735
    • MacKenzie, D.A.1    Carter, A.T.2    Wongwathanarat, P.3    Eagles, J.4    Salt, J.5    Archer, D.B.6
  • 37
    • 0029737878 scopus 로고    scopus 로고
    • Crystal structure of Delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins
    • Lindqvist Y, Huang W, Schneider G, Shanklin J (1996) Crystal structure of Delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins. Embo J 15:4081-4092
    • (1996) Embo J , vol.15 , pp. 4081-4092
    • Lindqvist, Y.1    Huang, W.2    Schneider, G.3    Shanklin, J.4
  • 38
    • 0035146189 scopus 로고    scopus 로고
    • Molecular cloning of full-length cDNA encoding Delta9 desaturase through PCR strategies and its genomic organization and expression in grass carp (Ctenopharyngodon idella)
    • Chang BE, Hsieh SL, Kuo CM (2001) Molecular cloning of full-length cDNA encoding Delta9 desaturase through PCR strategies and its genomic organization and expression in grass carp (Ctenopharyngodon idella). Mol Reprod Dev 58:245-254
    • (2001) Mol Reprod Dev , vol.58 , pp. 245-254
    • Chang, B.E.1    Hsieh, S.L.2    Kuo, C.M.3
  • 39
    • 33645506335 scopus 로고    scopus 로고
    • Identification of mouse palmitoyl-coenzyme a Delta9-desaturase
    • Miyazaki M, Bruggink SM, Ntambi JM (2006) Identification of mouse palmitoyl-coenzyme a Delta9-desaturase. J Lipid Res 47:700-704
    • (2006) J Lipid Res , vol.47 , pp. 700-704
    • Miyazaki, M.1    Bruggink, S.M.2    Ntambi, J.M.3
  • 40
    • 0016304096 scopus 로고
    • Escherichia coli ferredoxin, an iron-sulfur protein of the adrenodoxin type
    • Knoell HE, Knappe J (1974) Escherichia coli ferredoxin, an iron-sulfur protein of the adrenodoxin type. Eur J Biochem 50:245-252
    • (1974) Eur J Biochem , vol.50 , pp. 245-252
    • Knoell, H.E.1    Knappe, J.2


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