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Volumn 105, Issue 6, 2003, Pages 305-308

Enzyme-catalysed transphosphatidylation

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; PHOSPHOLIPASE D;

EID: 0038161132     PISSN: 14387697     EISSN: None     Source Type: Journal    
DOI: 10.1002/ejlt.200390060     Document Type: Short Survey
Times cited : (20)

References (17)
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    • (2000) Enzymes in Lipid Modification , pp. 219-262
    • Ulbrich-Hofmann, R.1
  • 2
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    • Phospholipase D - Structure, regulation and function
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    • Exton, J.H.1
  • 3
    • 0029928427 scopus 로고    scopus 로고
    • The transphosphatidylation activity of phospholipase D
    • Ch.-H. Yu, S.-Y. Liu, V. Panagia: The transphosphatidylation activity of phospholipase D. Mol. Cell. Biochem. 157 (1996) 101-105.
    • (1996) Mol. Cell. Biochem. , vol.157 , pp. 101-105
    • Yu, Ch.-H.1    Liu, S.-Y.2    Panagia, V.3
  • 4
    • 0031738656 scopus 로고    scopus 로고
    • Eukaryotic lipid-biosynthetic enzymes: The same but not the same
    • J. E. Vance: Eukaryotic lipid-biosynthetic enzymes: the same but not the same. TIBS 23 (1998) 423-428.
    • (1998) TIBS , vol.23 , pp. 423-428
    • Vance, J.E.1
  • 6
    • 0029921149 scopus 로고    scopus 로고
    • A novel family of phospholipase D homologues that includes phospholipid synthases and putative endonucleases: Identification of duplicated repeats and potential active site residues
    • C. P. Ponting, I. D. Kerr: A novel family of phospholipase D homologues that includes phospholipid synthases and putative endonucleases: Identification of duplicated repeats and potential active site residues. Protein Sci. 5 (1996) 914-922.
    • (1996) Protein Sci. , vol.5 , pp. 914-922
    • Ponting, C.P.1    Kerr, I.D.2
  • 7
    • 0033199570 scopus 로고    scopus 로고
    • Location of the catalytic nucleophile of phospholipase D of Streptomyces antibioticus in the C-terminal half domain
    • Y. Iwasaki, S. Horiike, K. Matsushima, T. Yamane: Location of the catalytic nucleophile of phospholipase D of Streptomyces antibioticus in the C-terminal half domain. Eur. J. Biochem. 264 (1999) 577-581.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 577-581
    • Iwasaki, Y.1    Horiike, S.2    Matsushima, K.3    Yamane, T.4
  • 8
    • 0033782386 scopus 로고    scopus 로고
    • The interdependence of solvent, acceptor alcohol and enzyme source in transphosphatidylation by phospholipase D
    • F. Hirche, R. Ulbrich-Hofmann: The interdependence of solvent, acceptor alcohol and enzyme source in transphosphatidylation by phospholipase D. Biocatal. Biotrans. 18 (2000) 343-353.
    • (2000) Biocatal. Biotrans. , vol.18 , pp. 343-353
    • Hirche, F.1    Ulbrich-Hofmann, R.2
  • 9
    • 0034162268 scopus 로고    scopus 로고
    • Multiple forms of phospholipase D in plants: The gene family, catalytic and regulatory properties, and cellular functions
    • X. Wang: Multiple forms of phospholipase D in plants: the gene family, catalytic and regulatory properties, and cellular functions. Progress Lipid Res. 39 (2000) 109-149.
    • (2000) Progress Lipid Res. , vol.39 , pp. 109-149
    • Wang, X.1
  • 12
    • 0034495516 scopus 로고    scopus 로고
    • Functional expression in insect cells, one-step purification and characterization of a recombinant phospholipase D from cowpea (Vigna unguiculata L. Walp)
    • H. El Maarouf, F. Carrière, M. Rivière, A. Abousalham: Functional expression in insect cells, one-step purification and characterization of a recombinant phospholipase D from cowpea (Vigna unguiculata L. Walp). Protein Eng. 13 (2000) 811-817.
    • (2000) Protein Eng. , vol.13 , pp. 811-817
    • El Maarouf, H.1    Carrière, F.2    Rivière, M.3    Abousalham, A.4
  • 13
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    • Hydrolytic and transphosphatidylation activities of phospholipase D from Savoy cabbage towards lysophosphatidylcholine
    • C. Virto, I. Svensson, P. Adlercreutz: Hydrolytic and transphosphatidylation activities of phospholipase D from Savoy cabbage towards lysophosphatidylcholine. Chem. Phys. Lipids 106 (2000) 41-51.
    • (2000) Chem. Phys. Lipids , vol.106 , pp. 41-51
    • Virto, C.1    Svensson, I.2    Adlercreutz, P.3
  • 15
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    • Alkylphospho-L-serine analogs: Synthesis of cytostatically active alkylphosphono derivatives
    • H. Brachwitz, M. Oelke, J. Bergmann, P. Langen: Alkylphospho-L-serine analogs: Synthesis of cytostatically active alkylphosphono derivatives. Bioorg. Med. Chem. Lett. 7 (1997) 1739-1742.
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 1739-1742
    • Brachwitz, H.1    Oelke, M.2    Bergmann, J.3    Langen, P.4
  • 16
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    • The interfacial pressure is an important parameter for the rate of phospholipase D catalyzed reactions in emulsion systems
    • F. Hirche, R. Ulbrich-Hofmann: The interfacial pressure is an important parameter for the rate of phospholipase D catalyzed reactions in emulsion systems. Biochim. Biophys. Acta 1436 (1999) 383-389
    • (1999) Biochim. Biophys. Acta , vol.1436 , pp. 383-389
    • Hirche, F.1    Ulbrich-Hofmann, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.