메뉴 건너뛰기




Volumn 27, Issue 1, 2012, Pages 78-83

The phenylthiourea is a competitive inhibitor of the enzymatic oxidation of DOPA by phenoloxidase

Author keywords

Enzyme inhibition; Melanization; Phenoloxidase; Phenylthiourea

Indexed keywords

DOPA; MONOPHENOL MONOOXYGENASE; PHENYLTHIOUREA;

EID: 84855367708     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.3109/14756366.2011.576010     Document Type: Article
Times cited : (53)

References (35)
  • 1
    • 0035999729 scopus 로고    scopus 로고
    • Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects
    • DOI 10.1034/j.1600-0749.2002.00056.x
    • Sugumaran M. Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Pigment Cell Res 2002;15:2-9. (Pubitemid 34535968)
    • (2002) Pigment Cell Research , vol.15 , Issue.1 , pp. 2-9
    • Sugumaran, M.1
  • 3
    • 0015766844 scopus 로고
    • A revised concept of mammalian melanogenesis: The possible synergistic functions of aerobic dopa oxidase and peroxidase. A review
    • Okun MR, Edelstein LM, Patel RP, Donnellan B. A revised concept of mammalian melanogenesis: the possible synergistic functions of aerobic dopa oxidase and peroxidase. A review. Yale J Biol Med 1973;46:535-540.
    • (1973) Yale J Biol Med , vol.46 , pp. 535-540
    • Okun, M.R.1    Edelstein, L.M.2    Patel, R.P.3    Donnellan, B.4
  • 4
    • 33749517866 scopus 로고    scopus 로고
    • Polyphenol oxidases in plants and fungi: Going places? A review
    • DOI 10.1016/j.phytochem.2006.08.006, PII S0031942206004560
    • Mayer AM. Polyphenol oxidases in plants and fungi: going places? A review. Phytochemistry 2006;67:2318-2331. (Pubitemid 44527933)
    • (2006) Phytochemistry , vol.67 , Issue.21 , pp. 2318-2331
    • Mayer, A.M.1
  • 5
    • 0000205628 scopus 로고
    • Mammalian tyrosinase; The relationship of copper to enzymatic activity
    • Lerner AB, Fitzpatrick TB, Calkins E, Summerson WH. Mammalian tyrosinase; the relationship of copper to enzymatic activity. J Biol Chem 1950;187:793-802.
    • (1950) J Biol Chem , vol.187 , pp. 793-802
    • Lerner, A.B.1    Fitzpatrick, T.B.2    Calkins, E.3    Summerson, W.H.4
  • 7
    • 0034804162 scopus 로고    scopus 로고
    • 2-peroxo)dicopper(II) complex: Mechanistic insight into the phenolase activity of tyrosinase [1]
    • DOI 10.1021/ja015702i
    • Itoh S, Kumei H, Taki M, Nagatomo S, Kitagawa T, Fukuzumi S. Oxygenation of phenols to catechols by a (mu-eta 2:eta 2-peroxo) dicopper(II) complex: mechanistic insight into the phenolase activity of tyrosinase. J Am Chem Soc 2001;123:6708-6709. (Pubitemid 32916470)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.27 , pp. 6708-6709
    • Itoh, S.1    Kumei, H.2    Taki, M.3    Nagatomo, S.4    Kitagawa, T.5    Fukuzumi, S.6
  • 8
    • 0000387352 scopus 로고
    • Competitive inhibitor binding to the binuclear copper site in tyrosinase
    • Winkler ME, Lerch K, Solomon EI. Competitive inhibitor binding to the binuclear copper site in tyrosinase. J Am Chem Soc 1981;103:7001-7003.
    • (1981) J Am Chem Soc , vol.103 , pp. 7001-7003
    • Winkler, M.E.1    Lerch, K.2    Solomon, E.I.3
  • 9
    • 44649198318 scopus 로고    scopus 로고
    • Analogues of N-hydroxy-N′-phenylthiourea and N-hydroxy-N′- phenylurea as inhibitors of tyrosinase and melanin formation
    • DOI 10.1016/j.bmcl.2008.04.079, PII S0960894X08004940
    • Criton M, Le Mellay-Hamon V. Analogues of N-hydroxy-N'-phenylthiourea and N-hydroxy-N'-phenylurea as inhibitors of tyrosinase and melanin formation. Bioorg Med Chem Lett 2008;18:3607-3610. (Pubitemid 351787563)
    • (2008) Bioorganic and Medicinal Chemistry Letters , vol.18 , Issue.12 , pp. 3607-3610
    • Criton, M.1    Le Mellay-Hamon, V.2
  • 10
    • 0001458215 scopus 로고    scopus 로고
    • Enzyme and metabolic inhibitors. (1963)
    • New York and London: Academic press
    • Webb JL. Enzyme and metabolic inhibitors. (1963). General principles of inhibition. New York and London: Academic press, pp. 156-194.
    • General Principles of Inhibition , pp. 156-194
    • Webb, J.L.1
  • 11
    • 0037080327 scopus 로고    scopus 로고
    • Identification of active site residues involved in metal cofactor binding and stereospecific substrate recognition in mammalian tyrosinase. Implications to the catalytic cycle
    • DOI 10.1021/bi011535n
    • Olivares C, García-Borrón JC, Solano F. Identification of active site residues involved in metal cofactor binding and stereospecific substrate recognition in Mammalian tyrosinase. Implications to the catalytic cycle. Biochemistry 2002;41:679-686. (Pubitemid 34062040)
    • (2002) Biochemistry , vol.41 , Issue.2 , pp. 679-686
    • Olivares, C.1    Garcia-Borron, J.C.2    Solano, F.3
  • 12
    • 0142214624 scopus 로고    scopus 로고
    • Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system
    • DOI 10.1021/ja036425d
    • Yamazaki S, Itoh S. Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system. J Am Chem Soc 2003;125:13034-13035. (Pubitemid 37305594)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.43 , pp. 13034-13035
    • Yamazaki, S.-I.1    Itoh, S.2
  • 13
    • 0034615509 scopus 로고    scopus 로고
    • Tyrosinase kinetics: A semi-quantitative model of the mechanism of oxidation of monohydric and dihydric phenolic substrates
    • DOI 10.1006/jtbi.1999.1061
    • Riley PA. Tyrosinase kinetics: a semi-quantitative model of the mechanism of oxidation of monohydric and dihydric phenolic substrates. J Theor Biol 2000;203:1-12. (Pubitemid 30658693)
    • (2000) Journal of Theoretical Biology , vol.203 , Issue.1 , pp. 1-12
    • Riley, P.A.1
  • 14
    • 0343485076 scopus 로고    scopus 로고
    • Hydroxylating activity of tyrosinase and its dependence on hydrogen peroxide
    • DOI 10.1006/abbi.1999.1519
    • Jiménez M, García-Carmona F. Hydroxylating activity of tyrosinase and its dependence on hydrogen peroxide. Arch Biochem Biophys 2000;373:255-260. (Pubitemid 30046512)
    • (2000) Archives of Biochemistry and Biophysics , vol.373 , Issue.1 , pp. 255-260
    • Jimenez, M.1    Garcia-Carmona, F.2
  • 16
    • 0027453615 scopus 로고
    • Effect of L-ascorbic acid on the monophenolase activity of tyrosinase
    • Ros JR, Rodríguez-López JN, García-Cánovas F. Effect of l-ascorbic acid on the monophenolase activity of tyrosinase. Biochem J 1993;295 (Pt 1):309-312. (Pubitemid 23298342)
    • (1993) Biochemical Journal , vol.295 , Issue.1 , pp. 309-312
    • Ros, J.R.1    Rodriguez-Lopez, J.N.2    Garcia-Canovas, F.3
  • 18
    • 33751500842 scopus 로고
    • Inhibition of kojic acid on polyphenol oxidase
    • Chen JS, Wei ChI, Marshall MR. Inhibition of kojic acid on polyphenol oxidase. J Agric Food Chem 1991;39(11):1897-1901.
    • (1991) J Agric Food Chem , vol.39 , Issue.11 , pp. 1897-1901
    • Chen, J.S.1    Chi, W.2    Marshall, M.R.3
  • 20
    • 2442555519 scopus 로고    scopus 로고
    • HPLC study of tyrosinase inhibition by thiopronine
    • DOI 10.1002/bmc.333
    • Girelli AM, Mattei E, Messina A. HPLC study of tyrosinase inhibition by thiopronine. Biomed Chromatogr 2004;18:436-442. (Pubitemid 39242750)
    • (2004) Biomedical Chromatography , vol.18 , Issue.7 , pp. 436-442
    • Girelli, A.M.1    Mattei, E.2    Messina, A.3
  • 21
    • 84855382676 scopus 로고
    • The action of phenylthiocarbamide on tyrosinase
    • Bernheim F, Bernheim MLC. The action of phenylthiocarbamide on tyrosinase. J Biol Chem 1942;8:213-217.
    • (1942) J Biol Chem , vol.8 , pp. 213-217
    • Bernheim, F.1    Bernheim, M.L.C.2
  • 22
    • 0345344572 scopus 로고
    • Studies on the mechanism of action of thiourea and related compounds; Inhibition of oxidative enzymes and oxidations catalyzed by copper
    • DuBois KP, Erway WF. Studies on the mechanism of action of thiourea and related compounds; inhibition of oxidative enzymes and oxidations catalyzed by copper. J Biol Chem 1946;165:711-721.
    • (1946) J Biol Chem , vol.165 , pp. 711-721
    • Dubois, K.P.1    Erway, W.F.2
  • 23
    • 0014295588 scopus 로고
    • Oxidation of phenolic compounds by Mycobacterium leprae and inhibition of phenolase by substrate analogues and copper chelators
    • Prabhakaran K, Kirchheimer WF, Harris EB. Oxidation of phenolic compounds by Mycobacterium leprae and inhibition of phenolase by substrate analogues and copper chelators. J Bacteriol 1968;95:2051-2053.
    • (1968) J Bacteriol , vol.95 , pp. 2051-2053
    • Prabhakaran, K.1    Kirchheimer, W.F.2    Harris, E.B.3
  • 25
    • 27844520797 scopus 로고    scopus 로고
    • Properties of phenoloxidase isolated from the cephalothorax of kuruma prawn (Penaeus japonicus)
    • DOI 10.1111/j.1745-4514.2005.00042.x
    • Benjakul S, Visessanguan W, Tanaka M. Properties of phenoloxidase isolated from the cephalothorax of kuruma prawn (Penaeus japonicus). J Food Biochem 2005;29:470-485. (Pubitemid 41639148)
    • (2005) Journal of Food Biochemistry , vol.29 , Issue.5 , pp. 470-485
    • Benjakul, S.1    Visessanguan, W.2    Tanaka, M.3
  • 27
    • 84855362891 scopus 로고
    • The action of phenyl-thiourea on melanogenesis in Xenopus laevis
    • Sims RT. The action of phenyl-thiourea on melanogenesis in Xenopus laevis. Quart J micr Sci 1962;103(4):439-446.
    • (1962) Quart J Micr Sci , vol.103 , Issue.4 , pp. 439-446
    • Sims, R.T.1
  • 29
    • 0025391978 scopus 로고
    • Effects of tyrosinase activity on the cytotoxicity of 3,4-dihydroxybenzylamine and buthionine sulfoximine in human melanoma cells
    • Prezioso JA, Fitzgerald GB, Wick MM. Effects of tyrosinase activity on the cytotoxicity of 3,4-dihydroxybenzylamine and buthionine sulfoximine in human melanoma cells. Pigment Cell Res 1990;3:49-54.
    • (1990) Pigment Cell Res , vol.3 , pp. 49-54
    • Prezioso, J.A.1    Fitzgerald, G.B.2    Wick, M.M.3
  • 31
    • 8644276533 scopus 로고    scopus 로고
    • Phenoloxidase activity in Apis mellifera honey bee pupae, and ecdysteroid-dependent expression of the prophenoloxidase mRNA
    • DOI 10.1016/j.ibmb.2004.08.005, PII S0965174804001511
    • Zufelato MS, Lourenço AP, Simões ZL, Jorge JA, Bitondi MM. Phenoloxidase activity in Apis mellifera honey bee pupae, and ecdysteroid-dependent expression of the prophenoloxidase mRNA. Insect Biochem Mol Biol 2004;34:1257-1268. (Pubitemid 39501037)
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , Issue.12 , pp. 1257-1268
    • Zufelato, M.S.1    Lourenco, A.P.2    Simoes, Z.L.P.3    Jorge, J.A.4    Bitondi, M.M.G.5
  • 32
    • 0028962450 scopus 로고
    • Highperformance liquid-chromatographic analysis of dopachrome and dihydroxyphenylalanine
    • Kågedal B, Konradsson P, Shibata T, Mishima Y. Highperformance liquid-chromatographic analysis of dopachrome and dihydroxyphenylalanine. Anal Biochem 1995;225: 264-269.
    • (1995) Anal Biochem , vol.225 , pp. 264-269
    • Kågedal, B.1    Konradsson, P.2    Shibata, T.3    Mishima, Y.4
  • 35
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • DOI 10.1038/4193
    • Klabunde T, Eicken C, Sacchettini JC, Krebs B. Crystal structure of a plant catechol oxidase containing a dicopper center. Nat Struct Biol 1998;5:1084-1090. (Pubitemid 28546272)
    • (1998) Nature Structural Biology , vol.5 , Issue.12 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sacchettini, J.C.3    Krebs, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.