메뉴 건너뛰기




Volumn 1804, Issue 11, 2010, Pages 2128-2135

Five monomeric hemocyanin subunits from Portunus trituberculatus: Purification, spectroscopic characterization, and quantitative evaluation of phenol monooxygenase activity

Author keywords

Arthropod; Cresolase; Hemocyanin; Oxygen activation; Phenol oxidase; Phenolase; Type III copper protein

Indexed keywords

BORIC ACID; CATECHOL; CATECHOL OXIDASE; COPPER DERIVATIVE; HEMOCYANIN; MONOMER; MONOPHENOL MONOOXYGENASE; OXYGENASE; PARA CRESOL; PHENOL MONOOXYGENASE; UNCLASSIFIED DRUG; UREA;

EID: 77956647755     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.08.003     Document Type: Article
Times cited : (15)

References (28)
  • 1
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • Cerenius L., Söderhäll K. The prophenoloxidase-activating system in invertebrates. Immunol. Rev. 2004, 198:116-126.
    • (2004) Immunol. Rev. , vol.198 , pp. 116-126
    • Cerenius, L.1    Söderhäll, K.2
  • 2
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase-activating system in invertebrate immunity
    • Söderhäll K., Cerenius L. Role of the prophenoloxidase-activating system in invertebrate immunity. Curr. Opin. Immunol. 1998, 10:23-28.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2
  • 5
    • 70350135449 scopus 로고    scopus 로고
    • Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes
    • Li Y.C., Wang Y., Jiang H.B., Deng J.P. Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes. Proc. Natl Acad. Sci. 2009, 106:17002-17006.
    • (2009) Proc. Natl Acad. Sci. , vol.106 , pp. 17002-17006
    • Li, Y.C.1    Wang, Y.2    Jiang, H.B.3    Deng, J.P.4
  • 6
    • 0000200878 scopus 로고
    • Recent structural work on the oxygen-transport protein hemocyanin
    • Magnus K.A., Tonthat H., Carpenter J.E. Recent structural work on the oxygen-transport protein hemocyanin. Chem. Rev. 1994, 94:727-735.
    • (1994) Chem. Rev. , vol.94 , pp. 727-735
    • Magnus, K.A.1    Tonthat, H.2    Carpenter, J.E.3
  • 8
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • Matoba Y., Kumagai T., Yamamoto A., Yoshitsu H., Sugiyama M. Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 2006, 281:8981-8990.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 9
    • 0027981519 scopus 로고
    • Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
    • Magnus K.A., Hazes B., Tonthat H., Bonaventura C., Bonaventura J., Hol W.G.J. Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins 1994, 19:302-309.
    • (1994) Proteins , vol.19 , pp. 302-309
    • Magnus, K.A.1    Hazes, B.2    Tonthat, H.3    Bonaventura, C.4    Bonaventura, J.5    Hol, W.G.J.6
  • 10
    • 1242343403 scopus 로고    scopus 로고
    • Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins
    • Decker H., Jaenicke E. Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins. Dev. Comp. Immunol. 2004, 28:673-687.
    • (2004) Dev. Comp. Immunol. , vol.28 , pp. 673-687
    • Decker, H.1    Jaenicke, E.2
  • 11
    • 0034255667 scopus 로고    scopus 로고
    • Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism
    • Decker H., Tuczek F. Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism. Trends Biochem. Sci. 2000, 25:392-397.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 392-397
    • Decker, H.1    Tuczek, F.2
  • 13
    • 50449088360 scopus 로고    scopus 로고
    • Phenoloxidase activity of hemocyanin in whiteleg shrimp Penaeus vannamei: conversion, characterization of catalytic properties, and role in postmortem melanosis
    • García-Carreño F.L., Cota K., Del Toro M.A.N. Phenoloxidase activity of hemocyanin in whiteleg shrimp Penaeus vannamei: conversion, characterization of catalytic properties, and role in postmortem melanosis. J. Agri. Food Chem. 2008, 56:6454-6459.
    • (2008) J. Agri. Food Chem. , vol.56 , pp. 6454-6459
    • García-Carreño, F.L.1    Cota, K.2    Del Toro, M.A.N.3
  • 14
    • 0032476016 scopus 로고    scopus 로고
    • Tarantula hemocyanin shows phenoloxidase activity
    • Decker H., Rimke T. Tarantula hemocyanin shows phenoloxidase activity. J. Biol. Chem. 1998, 273:25889-25892.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25889-25892
    • Decker, H.1    Rimke, T.2
  • 15
    • 0035658416 scopus 로고    scopus 로고
    • Hemocyanin a most likely inducer of black spots in kuruma prawn Penaeus japonicus during storage
    • Adachi K., Hirata T., Nagai K., Sakaguchi M. Hemocyanin a most likely inducer of black spots in kuruma prawn Penaeus japonicus during storage. J. Food Sci. 2001, 66:1130-1136.
    • (2001) J. Food Sci. , vol.66 , pp. 1130-1136
    • Adachi, K.1    Hirata, T.2    Nagai, K.3    Sakaguchi, M.4
  • 16
    • 0024287529 scopus 로고
    • Subunits of Panulirus japonicus hemocyanin.1. Isolation and properties
    • Makino N., Kimura S. Subunits of Panulirus japonicus hemocyanin.1. Isolation and properties. Eur. J. Biochem. 1988, 173:423-430.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 423-430
    • Makino, N.1    Kimura, S.2
  • 18
    • 0033233250 scopus 로고    scopus 로고
    • Spectroscopic properties of Carcinus aestuarii hemocyanin and its structural subunits
    • Dolashka-Angelova P., Hristova R., Stoeva S., Voelter W. Spectroscopic properties of Carcinus aestuarii hemocyanin and its structural subunits. Spectroc. Acta A 1999, 55:2927-2934.
    • (1999) Spectroc. Acta A , vol.55 , pp. 2927-2934
    • Dolashka-Angelova, P.1    Hristova, R.2    Stoeva, S.3    Voelter, W.4
  • 20
    • 77949357911 scopus 로고    scopus 로고
    • Catalytic oxygenation of phenols by arthropod hemocyanin, an oxygen carrier protein, from Portunus trituberculatus
    • Fujieda N., Yakiyama A., Itoh S. Catalytic oxygenation of phenols by arthropod hemocyanin, an oxygen carrier protein, from Portunus trituberculatus. Dalton Trans. 2010, 39:3083-3092.
    • (2010) Dalton Trans. , vol.39 , pp. 3083-3092
    • Fujieda, N.1    Yakiyama, A.2    Itoh, S.3
  • 21
    • 0142214624 scopus 로고    scopus 로고
    • Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system
    • Yamazaki S., Itoh S. Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system. J. Am. Chem. Soc. 2003, 125:13034-13035.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13034-13035
    • Yamazaki, S.1    Itoh, S.2
  • 23
    • 0024289914 scopus 로고
    • The subunit composition of Portunus trituberculatus hemocyanin polymers
    • Yoo B.S., Kim S.B., Lee J.H., Yang K.H. The subunit composition of Portunus trituberculatus hemocyanin polymers. Biochem. Biophys. Res. Commun. 1988, 153:748-752.
    • (1988) Biochem. Biophys. Res. Commun. , vol.153 , pp. 748-752
    • Yoo, B.S.1    Kim, S.B.2    Lee, J.H.3    Yang, K.H.4
  • 24
  • 26
    • 46849087354 scopus 로고    scopus 로고
    • Monooxygenase activity of Octopus vulgaris hemocyanin
    • Suzuki K., Shimokawa C., Morioka C., Itoh S. Monooxygenase activity of Octopus vulgaris hemocyanin. Biochemistry 2008, 47:7108-7115.
    • (2008) Biochemistry , vol.47 , pp. 7108-7115
    • Suzuki, K.1    Shimokawa, C.2    Morioka, C.3    Itoh, S.4
  • 27
    • 33744789676 scopus 로고    scopus 로고
    • Significant enhancement of monooxygenase activity of oxygen carrier protein hemocyanin by urea
    • Morioka C., Tachi Y., Suzuki S., Itoh S. Significant enhancement of monooxygenase activity of oxygen carrier protein hemocyanin by urea. J. Am. Chem. Soc. 2006, 128:6788-6789.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6788-6789
    • Morioka, C.1    Tachi, Y.2    Suzuki, S.3    Itoh, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.