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Volumn 1436, Issue 3, 1999, Pages 509-518

Affinities of various mammalian arachidonate lipoxygenases and cyclooxygenases for molecular oxygen as substrate

Author keywords

Arachidonic acid; Cyclooxygenase; Hypoxia; K(m) value for oxygen; Lipoxygenase

Indexed keywords

ARACHIDONATE 12 LIPOXYGENASE; ARACHIDONATE 15 LIPOXYGENASE; ARACHIDONATE 5 LIPOXYGENASE; ARACHIDONIC ACID; CATECHOL 2,3 DIOXYGENASE; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; OXYGEN; PROSTAGLANDIN SYNTHASE; RECOMBINANT ENZYME;

EID: 0344348865     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2760(98)00159-3     Document Type: Article
Times cited : (40)

References (41)
  • 1
    • 77956945079 scopus 로고
    • Enzymes in the biosynthesis and catabolism of the eicosanoids: Prostaglandins, thromboxanes, leukotrienes and hydroxy fatty acids
    • Pace-Asciak C.R., Smith W.L. Enzymes in the biosynthesis and catabolism of the eicosanoids: prostaglandins, thromboxanes, leukotrienes and hydroxy fatty acids. Enzymes. 16:1983;543-603.
    • (1983) Enzymes , vol.16 , pp. 543-603
    • Pace-Asciak, C.R.1    Smith, W.L.2
  • 2
    • 77956815952 scopus 로고
    • Enzymes in the arachidonic acid cascade
    • in: C. Pace-Asciak, E. Granström (Eds.) Elsevier Science, Amsterdam
    • S. Yamamoto, Enzymes in the arachidonic acid cascade, in: C. Pace-Asciak, E. Granström (Eds.), Prostaglandins and Related Substances, Elsevier Science, Amsterdam, 1983, pp. 171-202.
    • (1983) Prostaglandins and Related Substances , pp. 171-202
    • Yamamoto, S.1
  • 4
    • 0026480564 scopus 로고
    • Mammalian lipoxygenases: Molecular structures and functions
    • Yamamoto S. Mammalian lipoxygenases: molecular structures and functions. Biochim. Biophys. Acta. 1128:1992;117-131.
    • (1992) Biochim. Biophys. Acta , vol.1128 , pp. 117-131
    • Yamamoto, S.1
  • 5
    • 0025728865 scopus 로고
    • Prostaglandin endoperoxide synthase: Structure and catalysis
    • Smith W.L., Marnett L.J. Prostaglandin endoperoxide synthase: structure and catalysis. Biochim. Biophys. Acta. 1083:1991;1-17.
    • (1991) Biochim. Biophys. Acta , vol.1083 , pp. 1-17
    • Smith, W.L.1    Marnett, L.J.2
  • 7
    • 0017281663 scopus 로고
    • The steady-state kinetics of the oxygenation of linoleic acid catalysed by soybean lipoxygenase
    • Egmond M.R., Brunori M., Fasella P.M. The steady-state kinetics of the oxygenation of linoleic acid catalysed by soybean lipoxygenase. Eur. J. Biochem. 61:1976;93-100.
    • (1976) Eur. J. Biochem. , vol.61 , pp. 93-100
    • Egmond, M.R.1    Brunori, M.2    Fasella, P.M.3
  • 9
  • 11
    • 0027958244 scopus 로고
    • Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase
    • Suzuki H., Kishimoto K., Yoshimoto T., Yamamoto S., Kanai F., Ebina Y., Miyatake A., Tanabe T. Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase. Biochim. Biophys. Acta. 1210:1994;308-316.
    • (1994) Biochim. Biophys. Acta , vol.1210 , pp. 308-316
    • Suzuki, H.1    Kishimoto, K.2    Yoshimoto, T.3    Yamamoto, S.4    Kanai, F.5    Ebina, Y.6    Miyatake, A.7    Tanabe, T.8
  • 12
    • 0028076349 scopus 로고
    • Oxidative modification of human lipoproteins by lipoxygenases of different positional specificities
    • Kühn H., Belkner J., Suzuki H., Yamamoto S. Oxidative modification of human lipoproteins by lipoxygenases of different positional specificities. J. Lipid Res. 35:1994;1749-1759.
    • (1994) J. Lipid Res. , vol.35 , pp. 1749-1759
    • Kühn, H.1    Belkner, J.2    Suzuki, H.3    Yamamoto, S.4
  • 13
    • 0022977857 scopus 로고
    • Purification of arachidonate 5-lipoxygenase from porcine leukocytes and its reactivity with hydroperoxyeicosatetraenoic acids
    • Ueda N., Kaneko S., Yoshimoto T., Yamamoto S. Purification of arachidonate 5-lipoxygenase from porcine leukocytes and its reactivity with hydroperoxyeicosatetraenoic acids. J. Biol. Chem. 261:1986;7982-7988.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7982-7988
    • Ueda, N.1    Kaneko, S.2    Yoshimoto, T.3    Yamamoto, S.4
  • 14
    • 0030921521 scopus 로고    scopus 로고
    • A selective inhibitor of arachidonate 5-lipoxygenase scavenging peroxide activator
    • Suzuki H., Miyauchi D., Yamamoto S. A selective inhibitor of arachidonate 5-lipoxygenase scavenging peroxide activator. Biochem. Pharmacol. 54:1997;529-532.
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 529-532
    • Suzuki, H.1    Miyauchi, D.2    Yamamoto, S.3
  • 16
    • 0020023972 scopus 로고
    • Arachidonic acid-12-lipoxygenase from bovine platelets
    • Nugteren D.H. Arachidonic acid-12-lipoxygenase from bovine platelets. Methods Enzymol. 86:1982;49-54.
    • (1982) Methods Enzymol. , vol.86 , pp. 49-54
    • Nugteren, D.H.1
  • 17
    • 0002291563 scopus 로고
    • Cyclo-oxygenase: Measurement, purification and properties
    • in: A. Benedetto (Ed.) IRL Press, Washington, DC
    • R.J. Kulmacz, W.E.M. Lands, Cyclo-oxygenase: measurement, purification and properties, in: A. Benedetto (Ed.), Prostaglandins and Related Substances: A Practical Approach, IRL Press, Washington, DC, 1987, pp. 209-227.
    • (1987) Prostaglandins and Related Substances: A Practical Approach , pp. 209-227
    • Kulmacz, R.J.1    Lands, W.E.M.2
  • 18
    • 0022869485 scopus 로고
    • Arachidonate 12-lipoxygenase purified from porcine leukocytes by immunoaffinity chromatography and its reactivity with hydroperoxyeicosatetraenoic acids
    • Yokoyama C., Shinjo F., Yoshimoto T., Yamamoto S., Oates J.A., Brash A.R. Arachidonate 12-lipoxygenase purified from porcine leukocytes by immunoaffinity chromatography and its reactivity with hydroperoxyeicosatetraenoic acids. J. Biol. Chem. 261:1986;16714-16721.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16714-16721
    • Yokoyama, C.1    Shinjo, F.2    Yoshimoto, T.3    Yamamoto, S.4    Oates, J.A.5    Brash, A.R.6
  • 19
    • 0031556937 scopus 로고    scopus 로고
    • Induction of cyclooxygenase-1 in a human megakaryoblastic cell line (CMK) differentiated by phorbol ester
    • Ueda N., Yamashita R., Yamamoto S., Ishimura K. Induction of cyclooxygenase-1 in a human megakaryoblastic cell line (CMK) differentiated by phorbol ester. Biochim. Biophys. Acta. 1344:1997;103-110.
    • (1997) Biochim. Biophys. Acta , vol.1344 , pp. 103-110
    • Ueda, N.1    Yamashita, R.2    Yamamoto, S.3    Ishimura, K.4
  • 23
    • 0028942388 scopus 로고
    • Immediate responses of endothelial cells to hypoxia and reoxygenation: An in vitro model of cellular dysfunction
    • Watkins M.T., Haudenschild C.C., Al-Badawi H., Velazquez F.R., Larson D.M. Immediate responses of endothelial cells to hypoxia and reoxygenation: an in vitro model of cellular dysfunction. Am. J. Physiol. 268:1995;H749-H758.
    • (1995) Am. J. Physiol. , vol.268
    • Watkins, M.T.1    Haudenschild, C.C.2    Al-Badawi, H.3    Velazquez, F.R.4    Larson, D.M.5
  • 24
    • 0014217378 scopus 로고
    • On the specificity of the oxygenation of unsaturated fatty acids by soybean lipoxidase
    • Hamberg M., Samuelsson B. On the specificity of the oxygenation of unsaturated fatty acids by soybean lipoxidase. J. Biol. Chem. 242:1967;5329-5335.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5329-5335
    • Hamberg, M.1    Samuelsson, B.2
  • 25
    • 0029843150 scopus 로고    scopus 로고
    • Lipoxygenase reaction mechanism: Demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover
    • Glickman M.H., Klinman J.P. Lipoxygenase reaction mechanism: demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover. Biochemistry. 35:1996;12882-12892.
    • (1996) Biochemistry , vol.35 , pp. 12882-12892
    • Glickman, M.H.1    Klinman, J.P.2
  • 26
    • 0018402625 scopus 로고
    • Oxygenases and dioxygenases
    • in: F.L. Boschke (Ed.) Springer-Verlag, Berlin
    • M. Nozaki, Oxygenases and dioxygenases, in: F.L. Boschke (Ed.), Topics in Current Chemistry, Vol. 78, Springer-Verlag, Berlin, 1979, pp. 145-186.
    • (1979) Topics in Current Chemistry , vol.78 , pp. 145-186
    • Nozaki, M.1
  • 27
    • 0002132935 scopus 로고
    • Effects of heme substitution on the activity of heme-containing oxygenases
    • in: M. Nozaki, S. Yamamoto, Y. Ishimura, M.J. Coon, L. Ernster, R.W. Estabrook (Eds.) Academic Press, New York
    • R. Makino, T. Iizuka, K. Sakaguchi, Y. Ishimura, Effects of heme substitution on the activity of heme-containing oxygenases, in: M. Nozaki, S. Yamamoto, Y. Ishimura, M.J. Coon, L. Ernster, R.W. Estabrook (Eds.), Oxygenases and Oxygen Metabolism, Academic Press, New York, 1982, pp. 467-477.
    • (1982) Oxygenases and Oxygen Metabolism , pp. 467-477
    • Makino, R.1    Iizuka, T.2    Sakaguchi, K.3    Ishimura, Y.4
  • 28
    • 0025753586 scopus 로고
    • Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins
    • Hada T., Ueda N., Takahashi Y., Yamamoto S. Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins. Biochim. Biophys. Acta. 1083:1991;89-93.
    • (1991) Biochim. Biophys. Acta , vol.1083 , pp. 89-93
    • Hada, T.1    Ueda, N.2    Takahashi, Y.3    Yamamoto, S.4
  • 29
    • 0023754411 scopus 로고
    • Two immunologically and catalytically distinct arachidonate 12-lipoxygenases of bovine platelets and leukocytes
    • Takahashi Y., Ueda N., Yamamoto S. Two immunologically and catalytically distinct arachidonate 12-lipoxygenases of bovine platelets and leukocytes. Arch. Biochem. Biophys. 266:1988;613-621.
    • (1988) Arch. Biochem. Biophys. , vol.266 , pp. 613-621
    • Takahashi, Y.1    Ueda, N.2    Yamamoto, S.3
  • 30
    • 0021149826 scopus 로고
    • Studies on arachidonate 5-lipoxygenase of rat basophilic leukemia cells
    • Furukawa M., Yoshimoto T., Ochi K., Yamamoto S. Studies on arachidonate 5-lipoxygenase of rat basophilic leukemia cells. Biochim. Biophys. Acta. 795:1984;458-465.
    • (1984) Biochim. Biophys. Acta , vol.795 , pp. 458-465
    • Furukawa, M.1    Yoshimoto, T.2    Ochi, K.3    Yamamoto, S.4
  • 31
    • 0019791853 scopus 로고
    • Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes
    • Narumiya S., Salmon J.A., Cottee F.H., Weatherley B.C., Flower R.J. Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. J. Biol. Chem. 256:1981;9583-9592.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9583-9592
    • Narumiya, S.1    Salmon, J.A.2    Cottee, F.H.3    Weatherley, B.C.4    Flower, R.J.5
  • 33
    • 0017174218 scopus 로고
    • Steady-state kinetics of lipoxygenase oxygenation of unsaturated fatty acids
    • Gibian M.J., Galaway R.A. Steady-state kinetics of lipoxygenase oxygenation of unsaturated fatty acids. Biochemistry. 15:1976;4209-4214.
    • (1976) Biochemistry , vol.15 , pp. 4209-4214
    • Gibian, M.J.1    Galaway, R.A.2
  • 34
    • 2642670290 scopus 로고    scopus 로고
    • Oxygen concentration determines regiospecificity in soybean lipoxygenase-1 reaction via a branched kinetic scheme
    • Berry H., Débat H., Garde V.L. Oxygen concentration determines regiospecificity in soybean lipoxygenase-1 reaction via a branched kinetic scheme. J. Biol. Chem. 273:1998;2769-2776.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2769-2776
    • Berry, H.1    Débat, H.2    Garde, V.L.3
  • 35
    • 0022503366 scopus 로고
    • Enzymology and physiology of reticulocyte lipoxygenase: Comparison with other lipoxygenases
    • Schewe T., Rapoport S.M., Kühn H. Enzymology and physiology of reticulocyte lipoxygenase: comparison with other lipoxygenases. Adv. Enzymol. 58:1986;191-272.
    • (1986) Adv. Enzymol. , vol.58 , pp. 191-272
    • Schewe, T.1    Rapoport, S.M.2    Kühn, H.3
  • 37
    • 0025621521 scopus 로고
    • Oxygen partial pressure distribution within skeletal muscle: Indicator of whole body oxygen delivery in patients?
    • Boekstegers P., Riessen R., Seyde W. Oxygen partial pressure distribution within skeletal muscle: indicator of whole body oxygen delivery in patients? Adv. Exp. Med. Biol. 277:1990;507-514.
    • (1990) Adv. Exp. Med. Biol. , vol.277 , pp. 507-514
    • Boekstegers, P.1    Riessen, R.2    Seyde, W.3
  • 38
    • 0030034155 scopus 로고    scopus 로고
    • Brain tissue oxygen, carbon dioxide, and pH in neurosurgical patients at risk for ischemia
    • Hoffman W.E., Charbel F.T., Edelman G. Brain tissue oxygen, carbon dioxide, and pH in neurosurgical patients at risk for ischemia. Anesth. Analg. 82:1996;582-586.
    • (1996) Anesth. Analg. , vol.82 , pp. 582-586
    • Hoffman, W.E.1    Charbel, F.T.2    Edelman, G.3
  • 39
    • 0022444136 scopus 로고
    • Measurement of oxygen tension in the ischemic myocardium using encased polarographic oxygen electrodes
    • Barrett J.A., Lynch V.D., Balkon J., Wolf P.S. Measurement of oxygen tension in the ischemic myocardium using encased polarographic oxygen electrodes. J. Pharmacol. Methods. 15:1986;235-243.
    • (1986) J. Pharmacol. Methods , vol.15 , pp. 235-243
    • Barrett, J.A.1    Lynch, V.D.2    Balkon, J.3    Wolf, P.S.4
  • 40
    • 33750807106 scopus 로고    scopus 로고
    • Hypoxia does not directly stimulate ischemically sensitive abdominal visceral afferents during ischemia
    • Fu L.-W., Pan H.-L., Pitsillides K.F., Longhurst J.C. Hypoxia does not directly stimulate ischemically sensitive abdominal visceral afferents during ischemia. Am. J. Physiol. 271:1996;H261-H266.
    • (1996) Am. J. Physiol. , vol.271
    • Fu, L.-W.1    Pan, H.-L.2    Pitsillides, K.F.3    Longhurst, J.C.4
  • 41
    • 0025803078 scopus 로고
    • Differences in prostaglandin metabolism in cultured aortic and pulmonary arterial cells exposed to acute and chronic hypoxia
    • Farber H.W., Barnett H.F. Differences in prostaglandin metabolism in cultured aortic and pulmonary arterial cells exposed to acute and chronic hypoxia. Circ. Res. 68:1991;1446-1457.
    • (1991) Circ. Res. , vol.68 , pp. 1446-1457
    • Farber, H.W.1    Barnett, H.F.2


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