메뉴 건너뛰기




Volumn 189, Issue 4, 2008, Pages 407-410

Polyethylene glycol (PEG)-carboxylate-CoA synthetase is involved in PEG metabolism in Sphingopyxis macrogoltabida strain 103

Author keywords

Acyl CoA synthetase; Peg operon; Polyethylene glycol metabolism; Sphingopyxis macrogoltabida

Indexed keywords

ALDEHYDE DEHYDROGENASE; ENZYME; FATTY ACID; MACROGOL; POLYETHYLENE GLYCOL CARBOXYLATE COENZYME A SYNTHETASE;

EID: 43349103643     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-007-0320-z     Document Type: Article
Times cited : (7)

References (18)
  • 1
    • 33749625976 scopus 로고    scopus 로고
    • Dual regulation of a polyethylene glycol degradative operon by AraC-type and GalR-type regulators in Sphingopyxis macrogoltabida strain 103
    • Charoenpanich J, Tani A, Moriwaki N, Kimbara K, Kawai F (2006) Dual regulation of a polyethylene glycol degradative operon by AraC-type and GalR-type regulators in Sphingopyxis macrogoltabida strain 103. Microbiology 152:3025-3034
    • (2006) Microbiology , vol.152 , pp. 3025-3034
    • Charoenpanich, J.1    Tani, A.2    Moriwaki, N.3    Kimbara, K.4    Kawai, F.5
  • 2
    • 0030791144 scopus 로고    scopus 로고
    • Purification and characterization of an ether bond-cleaving enzyme involved in the metabolism of polyethylene glycol
    • Enokibara S, Kawai F (1997) Purification and characterization of an ether bond-cleaving enzyme involved in the metabolism of polyethylene glycol. J Ferment Bioeng 83:549-554
    • (1997) J Ferment Bioeng , vol.83 , pp. 549-554
    • Enokibara, S.1    Kawai, F.2
  • 6
    • 17644394208 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a periplasmic hydrolase for oxidized polyvinyl alcohol hydratase from Sphingomonas sp. strain 113P3
    • Klomklang W, Tani A, Kimbara K, Mamoto R, Ueda T, Shimao M, Kawai F (2005) Biochemical and molecular characterization of a periplasmic hydrolase for oxidized polyvinyl alcohol hydratase from Sphingomonas sp. strain 113P3. Microbiology 151:1255-1262
    • (2005) Microbiology , vol.151 , pp. 1255-1262
    • Klomklang, W.1    Tani, A.2    Kimbara, K.3    Mamoto, R.4    Ueda, T.5    Shimao, M.6    Kawai, F.7
  • 7
    • 0022613413 scopus 로고
    • Transport of long-chain fatty acids in Escherichia coli. Evidence for role of fadL gene product as long-chain fatty acid receptor
    • Nunn WD, Colburn RW, Black PN (1986) Transport of long-chain fatty acids in Escherichia coli. Evidence for role of fadL gene product as long-chain fatty acid receptor. J Biol Chem 261:167-171
    • (1986) J Biol Chem , vol.261 , pp. 167-171
    • Nunn, W.D.1    Colburn, R.W.2    Black, P.N.3
  • 8
    • 33745146505 scopus 로고    scopus 로고
    • Analysis of amino acid residues involved in catalysis of polyethylene glycol dehydrogenase from Sphingopyxis terrae, using three-dimensional molecular modeling-based kinetic characterization of mutants
    • Ohta T, Kawabata T, Nishikawa K, Tani A, Kimbara K, Kawai F (2006) Analysis of amino acid residues involved in catalysis of polyethylene glycol dehydrogenase from Sphingopyxis terrae, using three-dimensional molecular modeling-based kinetic characterization of mutants. Appl Environ Microbiol 72:4388-4396
    • (2006) Appl Environ Microbiol , vol.72 , pp. 4388-4396
    • Ohta, T.1    Kawabata, T.2    Nishikawa, K.3    Tani, A.4    Kimbara, K.5    Kawai, F.6
  • 9
    • 27644441493 scopus 로고    scopus 로고
    • A novel nicotinoprotein aldehyde dehydrogenase involved in polyethylene glycol degradation
    • Ohta T, Tani A, Kimbara K, Kawai F (2005) A novel nicotinoprotein aldehyde dehydrogenase involved in polyethylene glycol degradation. Appl Microbiol Biotechnol 68:639-646
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 639-646
    • Ohta, T.1    Tani, A.2    Kimbara, K.3    Kawai, F.4
  • 10
    • 0018611178 scopus 로고
    • Enzymatic microdetermination of serum free fatty acids
    • Shimizu S, Inoue K, Tani Y, Yamada H (1979) Enzymatic microdetermination of serum free fatty acids. Anal Biochem 98:341-345
    • (1979) Anal Biochem , vol.98 , pp. 341-345
    • Shimizu, S.1    Inoue, K.2    Tani, Y.3    Yamada, H.4
  • 11
    • 0034749531 scopus 로고    scopus 로고
    • The first step in polyethylene glycol degradation by Sphingomonads proceeds via a flavoprotein alcohol dehydrogenase containing flavin adenine dinucleotide
    • Sugimoto M, Tanabe M, Hataya M, Enokibara S, Duine JA, Kawai F (2001) The first step in polyethylene glycol degradation by Sphingomonads proceeds via a flavoprotein alcohol dehydrogenase containing flavin adenine dinucleotide. J Bacteriol 183:6694-6698
    • (2001) J Bacteriol , vol.183 , pp. 6694-6698
    • Sugimoto, M.1    Tanabe, M.2    Hataya, M.3    Enokibara, S.4    Duine, J.A.5    Kawai, F.6
  • 12
    • 33847208545 scopus 로고    scopus 로고
    • Structure and conservation of a polyethylene glycol-degradative operon in sphingomonads
    • Tani A, Charoenpanich J, Mori T, Takeichi M, Kimbara K, Kawai F (2007) Structure and conservation of a polyethylene glycol-degradative operon in sphingomonads. Microbiology 153:338-346
    • (2007) Microbiology , vol.153 , pp. 338-346
    • Tani, A.1    Charoenpanich, J.2    Mori, T.3    Takeichi, M.4    Kimbara, K.5    Kawai, F.6
  • 13
    • 2642522855 scopus 로고    scopus 로고
    • Crystal structure of the long-chain fatty acid transporter FadL
    • van den Berg B, Black PN, Clemons WMJ, Rapoport TA (2004) Crystal structure of the long-chain fatty acid transporter FadL. Science 304:1506-1509
    • (2004) Science , vol.304 , pp. 1506-1509
    • Van Den Berg, B.1    Black, P.N.2    Clemons, W.M.J.3    Rapoport, T.A.4
  • 14
    • 0037119475 scopus 로고    scopus 로고
    • Functional role of fatty acyl-coenzyme a synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport
    • Weimar JD, DiRusso CC, Delio R, Black PN (2002) Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport. J Biol Chem 277:29369-29376
    • (2002) J Biol Chem , vol.277 , pp. 29369-29376
    • Weimar, J.D.1    Dirusso, C.C.2    Delio, R.3    Black, P.N.4
  • 16
    • 9144224841 scopus 로고    scopus 로고
    • Cloning and expression of an ether-bond-cleaving enzyme involved in the metabolism of polyethylene glycol
    • Yamashita M, Tani A, Kawai F (2004a) Cloning and expression of an ether-bond-cleaving enzyme involved in the metabolism of polyethylene glycol. J Biosci Bioeng 98:313-315
    • (2004) J Biosci Bioeng , vol.98 , pp. 313-315
    • Yamashita, M.1    Tani, A.2    Kawai, F.3
  • 17
    • 9144268692 scopus 로고    scopus 로고
    • A new ether bond-splitting enzyme found in Gram-positive polyethylene glycol 6000-utilizing bacterium, Pseudonocardia sp. strain K1
    • Yamashita M, Tani A, Kawai F (2004b) A new ether bond-splitting enzyme found in Gram-positive polyethylene glycol 6000-utilizing bacterium, Pseudonocardia sp. strain K1. Appl Microbiol Biotechnol 66:174-179
    • (2004) Appl Microbiol Biotechnol , vol.66 , pp. 174-179
    • Yamashita, M.1    Tani, A.2    Kawai, F.3
  • 18
    • 0037507257 scopus 로고    scopus 로고
    • Vectorial acylation in Saccharomyces cerevisiae. Fat1p and fatty acyl-CoA synthetase are interacting components of a fatty acid import complex
    • Zou Z, Tong F, Faergeman NJ, Borsting C, Black PN, DiRusso CC (2003) Vectorial acylation in Saccharomyces cerevisiae. Fat1p and fatty acyl-CoA synthetase are interacting components of a fatty acid import complex. J Biol Chem 278:16414-16422
    • (2003) J Biol Chem , vol.278 , pp. 16414-16422
    • Zou, Z.1    Tong, F.2    Faergeman, N.J.3    Borsting, C.4    Black, P.N.5    Dirusso, C.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.