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Volumn 260, Issue 3, 1999, Pages 794-800

Half-of-the-sites reactivity of outer-membrane phospholipase A against an active-site-directed inhibitor

Author keywords

Half of the sites reactivity; Inhibition; Outer membrane; Phospholipase; Phosphonate

Indexed keywords

1,4 NITROPHENYLOCTYLPHOSPHONATE 2 TRIDECYLCARBAMOYL 3 ETHANESULFONYLAMINO 3 DEOXYGLYCEROL; ENZYME INHIBITOR; PHOSPHOLIPASE A; UNCLASSIFIED DRUG;

EID: 0242508142     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00221.x     Document Type: Article
Times cited : (5)

References (35)
  • 1
    • 0015518155 scopus 로고
    • Two kinds of phospholipase A and lysophospholipase in Escherichia coli
    • Doi, O., Ohki, M. & Nojima, S. (1973) Two kinds of phospholipase A and lysophospholipase in Escherichia coli. Biochim. Biophys. Acta 260, 244-258.
    • (1973) Biochim. Biophys. Acta , vol.260 , pp. 244-258
    • Doi, O.1    Ohki, M.2    Nojima, S.3
  • 3
    • 0030949536 scopus 로고    scopus 로고
    • Molecular characteriziation of pldA, the structural gene for a phospholipase A from Campylobacter coli, and its contribution to cell-associated hemolysis
    • Grant, K.A., Ubarretxena-Belandia, I., Dekker, N., Richardson, P.T. & Park, S.F. (1997) Molecular characteriziation of pldA, the structural gene for a phospholipase A from Campylobacter coli, and its contribution to cell-associated hemolysis. Infect, Immun. 65, 1172-1180.
    • (1997) Infect, Immun. , vol.65 , pp. 1172-1180
    • Grant, K.A.1    Ubarretxena-Belandia, I.2    Dekker, N.3    Richardson, P.T.4    Park, S.F.5
  • 4
    • 0032197579 scopus 로고    scopus 로고
    • Sequence comparison of outer membrane phospholipase A: Implications for structure and catalytic mechanism
    • Brok, R.G.P.M., Boots, A.P., Dekker, N., Verheij, H.M. & Tommassen, J. (1998) Sequence comparison of outer membrane phospholipase A: implications for structure and catalytic mechanism. Res. Microbiol. 149, 703-710.
    • (1998) Res. Microbiol. , vol.149 , pp. 703-710
    • Brok, R.G.P.M.1    Boots, A.P.2    Dekker, N.3    Verheij, H.M.4    Tommassen, J.5
  • 5
    • 0024235789 scopus 로고
    • Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: Identity of protease VII and OmpT
    • Sugimura, K. & Nishihara, T. (1988) Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: Identity of protease VII and OmpT. J. Bacteriol. 170, 5625-5632.
    • (1988) J. Bacteriol. , vol.170 , pp. 5625-5632
    • Sugimura, K.1    Nishihara, T.2
  • 6
    • 0028040011 scopus 로고
    • New outer membrane-associated protease of Escherichia coli K-12
    • Kaufmann, A., Stierhof, Y.-D. & Henning, U. (1994) New outer membrane-associated protease of Escherichia coli K-12. J. Bacteriol. 176, 359-367.
    • (1994) J. Bacteriol. , vol.176 , pp. 359-367
    • Kaufmann, A.1    Stierhof, Y.-D.2    Henning, U.3
  • 7
    • 0018534736 scopus 로고
    • Properties of purified detergent-resistant phospholipase A of Escherichia coli K-12. Inactivation and protection with detergents and phospholipids
    • Tamori, Y., Nishijima, M. & Nojima, S. (1979) Properties of purified detergent-resistant phospholipase A of Escherichia coli K-12. Inactivation and protection with detergents and phospholipids. J. Biochem. (Tokyo) 86, 1129-1138.
    • (1979) J. Biochem. (Tokyo) , vol.86 , pp. 1129-1138
    • Tamori, Y.1    Nishijima, M.2    Nojima, S.3
  • 8
    • 0024505578 scopus 로고
    • Kinetic characterization of Escherichia coli outer membrane phospholipase A using mixed detergent-lipid micelles
    • Horrevoets, A.J.G., Hackeng, T.M., Verheij, H.M., Dijkman, R. & de Haas, G.H. (1989) Kinetic characterization of Escherichia coli outer membrane phospholipase A using mixed detergent-lipid micelles. Biochemistry 28, 1139-1147.
    • (1989) Biochemistry , vol.28 , pp. 1139-1147
    • Horrevoets, A.J.G.1    Hackeng, T.M.2    Verheij, H.M.3    Dijkman, R.4    De Haas, G.H.5
  • 9
    • 0025780096 scopus 로고
    • Inactivation of Escherichia coli outer-membrane phospholipase A by the affinity label hexadecanesulfonyl fluoride. Evidence for an active site serine
    • Horrevoets, A.J.G., Verheij, H.M. & de Haas, G.H. (1991) Inactivation of Escherichia coli outer-membrane phospholipase A by the affinity label hexadecanesulfonyl fluoride. Evidence for an active site serine. Eur. J. Biochem. 198, 247-253.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 247-253
    • Horrevoets, A.J.G.1    Verheij, H.M.2    De Haas, G.H.3
  • 10
    • 0029894754 scopus 로고    scopus 로고
    • Escherichia coli outer membrane phospholipase A: Role of two serines in enzymatic activity
    • Brok, R.G.P.M., Ubarretxena-Belandia, I., Dekker, N., Tommassen, J. & Verheij, H.M. (1996) Escherichia coli outer membrane phospholipase A: role of two serines in enzymatic activity. Biochemistry 35, 7787-7793.
    • (1996) Biochemistry , vol.35 , pp. 7787-7793
    • Brok, R.G.P.M.1    Ubarretxena-Belandia, I.2    Dekker, N.3    Tommassen, J.4    Verheij, H.M.5
  • 11
    • 0029618716 scopus 로고
    • A conserved histidine residue of Escheichia coli outer membrane phospholipase A is important for activity
    • Brok, R.G.P.M., Dekker, N., Gerrits, N., Verheij, H.M. & Tommassen, J. (1995) A conserved histidine residue of Escheichia coli outer membrane phospholipase A is important for activity. Eur. J. Biochem. 234, 934-938.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 934-938
    • Brok, R.G.P.M.1    Dekker, N.2    Gerrits, N.3    Verheij, H.M.4    Tommassen, J.5
  • 12
    • 0028223392 scopus 로고
    • Structure and function of lipases
    • Derewenda, Z.S. (1994) Structure and function of lipases. Adv. Protein Chem. 45, 1-51.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 1-51
    • Derewenda, Z.S.1
  • 13
    • 0031013983 scopus 로고    scopus 로고
    • Dimerization regulates the enzymatic activity of outer membrane phospholipase A
    • Dekker, N., Tommassen, J., Lustig, A., Rosenbusch, J.P. & Verheij, H.M. (1997) Dimerization regulates the enzymatic activity of outer membrane phospholipase A. J. Biol. Chem. 272, 3179-3184.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3179-3184
    • Dekker, N.1    Tommassen, J.2    Lustig, A.3    Rosenbusch, J.P.4    Verheij, H.M.5
  • 14
    • 0028980657 scopus 로고
    • Crystallization and preliminary X-ray analysis of outer membrane phospholipase A from Escherichia coli
    • Blaauw, M., Dekker, N., Verheij, H.M., Kalk, K.H. & Dijkstra, B.W. (1995) Crystallization and preliminary X-ray analysis of outer membrane phospholipase A from Escherichia coli. FEBS Lett. 373, 10-12.
    • (1995) FEBS Lett. , vol.373 , pp. 10-12
    • Blaauw, M.1    Dekker, N.2    Verheij, H.M.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 17
    • 0025668794 scopus 로고
    • Crystal structure of Bee-Venom phospholipase A2 in a complex with a transition-state analogue
    • Scott, D.L., Otwinowski, Z., Gelb, M.H. & Sigler, P.B. (1990) Crystal structure of Bee-Venom phospholipase A2 in a complex with a transition-state analogue Science 250, 1563-1566.
    • (1990) Science , vol.250 , pp. 1563-1566
    • Scott, D.L.1    Otwinowski, Z.2    Gelb, M.H.3    Sigler, P.B.4
  • 19
    • 0029101182 scopus 로고
    • In vitro folding of Escherichia coli outer membrane phospholipase A
    • Dekker, N., Merck, K., Tommassen, J. & Verheij, H.M. (1995) In vitro folding of Escherichia coli outer membrane phospholipase A. Eur. J. Biochem. 232, 214-219.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 214-219
    • Dekker, N.1    Merck, K.2    Tommassen, J.3    Verheij, H.M.4
  • 20
    • 0030432417 scopus 로고    scopus 로고
    • The lipase from Staphylococcus aureus: Expression in Escherichia coli large-scale purification and comparison of substrate specificity to Staphylococcus hyicus lipase
    • Simons, J.-W.F.A., Adams, H., Cox, R.C., Dekker, N., Götz, F., Slotboom, A.J. & Verheij, H.M. (1996) The lipase from Staphylococcus aureus: expression in Escherichia coli large-scale purification and comparison of substrate specificity to Staphylococcus hyicus lipase. Eur. J. Biochem. 242, 760-769.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 760-769
    • Simons, J.-W.F.A.1    Adams, H.2    Cox, R.C.3    Dekker, N.4    Götz, F.5    Slotboom, A.J.6    Verheij, H.M.7
  • 21
    • 0016855087 scopus 로고
    • The interaction of phospholipase A2 with micellar interfaces. The role of the N-terminal region
    • van Dam-Mieras, M.C.E., Slotboom, A.J., Pieterson, W.A. & de Haas, G.H. (1975) The interaction of phospholipase A2 with micellar interfaces. The role of the N-terminal region. Biochemistry 14, 5387-5394.
    • (1975) Biochemistry , vol.14 , pp. 5387-5394
    • Van Dam-Mieras, M.C.E.1    Slotboom, A.J.2    Pieterson, W.A.3    De Haas, G.H.4
  • 22
    • 0017130565 scopus 로고
    • Studies on lysophospholipases VII: Synthesis of acylthioester analogs of lysolecithin and their use in a continuous spectrophotometric assay for lysophospholipases, a method with potential applicability to other lipolytic enzymes
    • Aarsman, A.J., van Deemen, L.L.M. & van den Bosch, H. (1976) Studies on lysophospholipases VII: Synthesis of acylthioester analogs of lysolecithin and their use in a continuous spectrophotometric assay for lysophospholipases, a method with potential applicability to other lipolytic enzymes. Bioorg. Chem. 5, 241-253.
    • (1976) Bioorg. Chem. , vol.5 , pp. 241-253
    • Aarsman, A.J.1    Van Deemen, L.L.M.2    Van den Bosch, H.3
  • 23
    • 0013598570 scopus 로고
    • An improved method for the preparation of 1,2-isopropylidene-sn-glycerol Chem
    • Eibl, H. (1981) An improved method for the preparation of 1,2-isopropylidene-sn-glycerol Chem. Phys. Lipids 28, 1-5.
    • (1981) Phys. Lipids , vol.28 , pp. 1-5
    • Eibl, H.1
  • 25
    • 0000919625 scopus 로고
    • A facile procedure for the synthesis of saturated phosphatidylcholines
    • Hermetter, A. & Paltauf, F. (1981) A facile procedure for the synthesis of saturated phosphatidylcholines. Chem. Phys. Lipids 28, 111-115.
    • (1981) Chem. Phys. Lipids , vol.28 , pp. 111-115
    • Hermetter, A.1    Paltauf, F.2
  • 27
    • 0000171590 scopus 로고
    • The kinetics of the α-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetate
    • Kezdy, F.J. & Bender, M.L. (1962) The kinetics of the α-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry 1, 1097-1106.
    • (1962) Biochemistry , vol.1 , pp. 1097-1106
    • Kezdy, F.J.1    Bender, M.L.2
  • 28
    • 0015994917 scopus 로고
    • pH dependence of chymotrypsin catalysis. Appendix: Substrate binding to dimeric alpha-chymotrypsin studied by x-ray diffraction and the equilibrium method
    • Fersht, A.R. & Renard, M. (1974) pH dependence of chymotrypsin catalysis. Appendix: substrate binding to dimeric alpha-chymotrypsin studied by x-ray diffraction and the equilibrium method. Biochemistry 13, 1416-1420.
    • (1974) Biochemistry , vol.13 , pp. 1416-1420
    • Fersht, A.R.1    Renard, M.2
  • 29
  • 30
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut, J. (1977) Serine proteases: structure and mechanism of catalysis. Annu. Rev. Biochem. 46, 331-358.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 331-358
    • Kraut, J.1
  • 31
    • 0021126688 scopus 로고
    • Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetyl thiocholine
    • Froede, H.C. & Wilson, I.B. (1984) Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetyl thiocholine. J. Biol. Chem. 259, 11010-11013.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11010-11013
    • Froede, H.C.1    Wilson, I.B.2
  • 35
    • 0014352175 scopus 로고
    • Negative cooperativity in enzyme action. The binding diphosphopyridine nucleotide to glyceraldehyde 3-phosphate dehydrogenase
    • Conway, A. & Koshland, D.E. (1968) Negative cooperativity in enzyme action. The binding diphosphopyridine nucleotide to glyceraldehyde 3-phosphate dehydrogenase. Biochemistry 7, 4011-4023.
    • (1968) Biochemistry , vol.7 , pp. 4011-4023
    • Conway, A.1    Koshland, D.E.2


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