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Volumn 21, Issue 1, 2014, Pages 13-19

Tyrosine metabolic enzymes from insects and mammals: A comparative perspective

Author keywords

Arylalkylamine N acetyltransferase (aaNAT); Enzymology; L DOPA decarboxylase (DDC); Melanogenesis; Tyrosine metabolism

Indexed keywords

ENZYME; INSECT PROTEIN; MELANIN; TYROSINE;

EID: 84892156331     PISSN: 16729609     EISSN: 17447917     Source Type: Journal    
DOI: 10.1111/1744-7917.12038     Document Type: Review
Times cited : (51)

References (46)
  • 2
    • 0031899713 scopus 로고    scopus 로고
    • Levodopa-is toxicity a myth?
    • Agid, Y. (1998) Levodopa-is toxicity a myth? Neurology, 50, 858-863.
    • (1998) Neurology , vol.50 , pp. 858-863
    • Agid, Y.1
  • 3
    • 0007949877 scopus 로고
    • Phenoloxidases and the integument
    • eds. K. Binnington & A. Retnakaran) - CSIRO, Australia.
    • Barrett, F.M. (1991) Phenoloxidases and the integument. Physiology of the Insect Epidermis (eds. K. Binnington & A. Retnakaran), pp. 195-212. CSIRO, Australia.
    • (1991) Physiology of the Insect Epidermis , pp. 195-212
    • Barrett, F.M.1
  • 5
    • 0031690595 scopus 로고    scopus 로고
    • Human tyrosinase related protein-1 (TRP-1) does not function as a DHICA oxidase activity in contrast to murine TRP-1
    • Boissy, R.E., Sakai, C., Zhao, H., Kobayashi, T. and Hearing, V.J. (1998) Human tyrosinase related protein-1 (TRP-1) does not function as a DHICA oxidase activity in contrast to murine TRP-1. Experimental Dermatology, 7, 198-204.
    • (1998) Experimental Dermatology , vol.7 , pp. 198-204
    • Boissy, R.E.1    Sakai, C.2    Zhao, H.3    Kobayashi, T.4    Hearing, V.J.5
  • 8
    • 0141638380 scopus 로고    scopus 로고
    • 3,4-Dihydroxyphenylacetaldehyde is the toxic dopamine metabolite in vivo: implications for Parkinson's disease pathogenesis
    • Burke, W.J., Li, S.W., Williams, E.A., Nonneman, R. and Zahm, D.S. (2003) 3, 4-Dihydroxyphenylacetaldehyde is the toxic dopamine metabolite in vivo: implications for Parkinson's disease pathogenesis. Brain Research, 989, 205-213.
    • (2003) Brain Research , vol.989 , pp. 205-213
    • Burke, W.J.1    Li, S.W.2    Williams, E.A.3    Nonneman, R.4    Zahm, D.S.5
  • 10
    • 2642525364 scopus 로고    scopus 로고
    • What are the essential elements needed for the determination of amino acid requirements in humans?
    • Furst, P. and Stehle, P. (2004) What are the essential elements needed for the determination of amino acid requirements in humans? Journal of Nutrition, 134, 1558-1565.
    • (2004) Journal of Nutrition , vol.134 , pp. 1558-1565
    • Furst, P.1    Stehle, P.2
  • 11
    • 0037113251 scopus 로고    scopus 로고
    • Identification of Drosophila melanogaster yellow-f and yellow-f2 proteins as dopachrome-conversion enzymes
    • Han, Q., Fang, J., Ding, H., Johnson, J.K., Christensen, B.M. and Li, J. (2002) Identification of Drosophila melanogaster yellow-f and yellow-f2 proteins as dopachrome-conversion enzymes. Biochemical Journal, 368, 333-340.
    • (2002) Biochemical Journal , vol.368 , pp. 333-340
    • Han, Q.1    Fang, J.2    Ding, H.3    Johnson, J.K.4    Christensen, B.M.5    Li, J.6
  • 12
    • 77952475277 scopus 로고    scopus 로고
    • Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase
    • Han, Q., Ding, H., Robinson, H., Christensen, B.M. and Li, J. (2010) Crystal structure and substrate specificity of Drosophila 3, 4-dihydroxyphenylalanine decarboxylase. PLoS ONE, 5, e8826.
    • (2010) PLoS ONE , vol.5
    • Han, Q.1    Ding, H.2    Robinson, H.3    Christensen, B.M.4    Li, J.5
  • 15
    • 30844445750 scopus 로고    scopus 로고
    • Dopa decarboxylase: a model gene-enzyme system for studying development, behavior, and systematics
    • Hodgetts, R.B. and O'Keefe, S.L. (2006) Dopa decarboxylase: a model gene-enzyme system for studying development, behavior, and systematics. Annual Review of Entomology, 51, 259-284.
    • (2006) Annual Review of Entomology , vol.51 , pp. 259-284
    • Hodgetts, R.B.1    O'Keefe, S.L.2
  • 16
    • 0019995407 scopus 로고
    • N-β-alanyldopamine: major role in insect cuticle tanning
    • Hopkins, T.L., Morgan, T.D., Aso, Y. and Kramer, K.J. (1982). N-β-alanyldopamine: major role in insect cuticle tanning. Science, 217, 364-366.
    • (1982) Science , vol.217 , pp. 364-366
    • Hopkins, T.L.1    Morgan, T.D.2    Aso, Y.3    Kramer, K.J.4
  • 17
    • 0037902622 scopus 로고    scopus 로고
    • The IFPCS presidential lecture: a chemist's view of melanogenesis
    • Ito, S. (2003) The IFPCS presidential lecture: a chemist's view of melanogenesis. Pigment Cell Research, 16, 230-236.
    • (2003) Pigment Cell Research , vol.16 , pp. 230-236
    • Ito, S.1
  • 18
    • 0034816028 scopus 로고    scopus 로고
    • Cloning and characterization of a dopachrome conversion enzyme from the yellow fever mosquito, Aedes aegypti
    • Johnson, J.K., Li, J. and Christensen, B.M. (2001) Cloning and characterization of a dopachrome conversion enzyme from the yellow fever mosquito, Aedes aegypti. Insect Biochemistry and Molecular Biology, 31, 1125-1135.
    • (2001) Insect Biochemistry and Molecular Biology , vol.31 , pp. 1125-1135
    • Johnson, J.K.1    Li, J.2    Christensen, B.M.3
  • 19
    • 0001012621 scopus 로고
    • N-acetyldopamine as sclerotizing agent of the insect cuticle
    • Karlson, P. and Sekeris, C.E. (1962) N-acetyldopamine as sclerotizing agent of the insect cuticle. Nature, 195, 183-184.
    • (1962) Nature , vol.195 , pp. 183-184
    • Karlson, P.1    Sekeris, C.E.2
  • 20
    • 17444384890 scopus 로고    scopus 로고
    • Identification and molecular characterization of a prophenoloxidase involved in Aedes aegypti chorion melanization
    • Kim, S.R., Yao, R., Han, Q., Christensen, B.M. and Li, J. (2005) Identification and molecular characterization of a prophenoloxidase involved in Aedes aegypti chorion melanization. Insect Molecular Biology, 14, 185-194.
    • (2005) Insect Molecular Biology , vol.14 , pp. 185-194
    • Kim, S.R.1    Yao, R.2    Han, Q.3    Christensen, B.M.4    Li, J.5
  • 22
    • 84872682151 scopus 로고    scopus 로고
    • Biological function of insect yellow gene family
    • (eds. T.-X. Liu & L. Kang), Higher Education Press, Beijing.
    • Li, J. and Christensen, B.M. (2012) Biological function of insect yellow gene family. Recent Advances in Entomological Research (eds. T.-X. Liu & L. Kang), pp 121-131. Higher Education Press, Beijing.
    • (2012) Recent Advances in Entomological Research , pp. 121-131
    • Li, J.1    Christensen, B.M.2
  • 23
    • 26244443507 scopus 로고    scopus 로고
    • Purification and primary structural characterization of prophenoloxidases from Aedes aegypti larvae
    • Li, J.S., Ruyl Kim, S., Christensen, B.M. and Li, J. (2005) Purification and primary structural characterization of prophenoloxidases from Aedes aegypti larvae. Insect Biochemistry and Molecular Biology, 35, 1269-1283.
    • (2005) Insect Biochemistry and Molecular Biology , vol.35 , pp. 1269-1283
    • Li, J.S.1    Ruyl Kim, S.2    Christensen, B.M.3    Li, J.4
  • 24
    • 34547855844 scopus 로고    scopus 로고
    • Proteomic analysis of N-glycosylation in mosquito dopachrome conversion enzyme
    • Li, J.S., Vavricka, C.J., Christensen, B.M. and Li, J. (2007) Proteomic analysis of N-glycosylation in mosquito dopachrome conversion enzyme. Proteomics, 7, 2557-2569.
    • (2007) Proteomics , vol.7 , pp. 2557-2569
    • Li, J.S.1    Vavricka, C.J.2    Christensen, B.M.3    Li, J.4
  • 26
    • 79952608066 scopus 로고    scopus 로고
    • Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations
    • Mehere, P., Han, Q., Lemkul, J.A., Vavricka, C.J., Robinson, H., Bevan, D.R. and Li, J. (2010) Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations. Protein & Cell, 1, 1023-1032.
    • (2010) Protein & Cell , vol.1 , pp. 1023-1032
    • Mehere, P.1    Han, Q.2    Lemkul, J.A.3    Vavricka, C.J.4    Robinson, H.5    Bevan, D.R.6    Li, J.7
  • 27
    • 79959799364 scopus 로고    scopus 로고
    • Identification and characterization of two arylalkylamine N-acetyltransferases in the yellow fever mosquito, Aedes aegypti
    • Mehere, P., Han, Q., Christensen, B.M. and Li, J. (2011) Identification and characterization of two arylalkylamine N-acetyltransferases in the yellow fever mosquito, Aedes aegypti. Insect Biochemistry and Molecular Biology, 41, 707-714.
    • (2011) Insect Biochemistry and Molecular Biology , vol.41 , pp. 707-714
    • Mehere, P.1    Han, Q.2    Christensen, B.M.3    Li, J.4
  • 29
    • 0026021079 scopus 로고
    • Dopa-responsive dystonia: long-term treatment response and prognosis
    • Nygaard, T.G., Marsden, C.D. and Fahn, S. (1991) Dopa-responsive dystonia: long-term treatment response and prognosis. Neurology, 41, 174-181.
    • (1991) Neurology , vol.41 , pp. 174-181
    • Nygaard, T.G.1    Marsden, C.D.2    Fahn, S.3
  • 31
    • 0018251759 scopus 로고
    • 5,6-Dihydroxyindole is a melanin precursor showing potent cytotoxicity
    • Pawelek, J.M. and Lerner, A.B. (1978) 5, 6-Dihydroxyindole is a melanin precursor showing potent cytotoxicity. Nature, 276, 626-628.
    • (1978) Nature , vol.276 , pp. 626-628
    • Pawelek, J.M.1    Lerner, A.B.2
  • 33
    • 0024285098 scopus 로고
    • A novel quinone: quinone methide isomerase generates quinone methides in insect cuticle
    • Saul, S. and Sugumaran, M. (1988) A novel quinone: quinone methide isomerase generates quinone methides in insect cuticle. FEBS Letters, 237, 155-158.
    • (1988) FEBS Letters , vol.237 , pp. 155-158
    • Saul, S.1    Sugumaran, M.2
  • 34
    • 0024353898 scopus 로고
    • Characterization of a new enzyme system that desaturates the side chain of N-acetyldopamine
    • Saul, S. and Sugumaran, M. (1989) Characterization of a new enzyme system that desaturates the side chain of N-acetyldopamine. FEBS Letters, 251, 69-73.
    • (1989) FEBS Letters , vol.251 , pp. 69-73
    • Saul, S.1    Sugumaran, M.2
  • 35
    • 0013887495 scopus 로고
    • Dopa decarboxylase: substrates, coenzyme, inhibitors
    • Sourkes, T.L. (1966) Dopa decarboxylase: substrates, coenzyme, inhibitors. Pharmacological Reviews, 18, 53-60.
    • (1966) Pharmacological Reviews , vol.18 , pp. 53-60
    • Sourkes, T.L.1
  • 36
    • 0026426696 scopus 로고
    • Molecular mechanisms for mammalian melanogenesis. Comparison with insect cuticle sclerotization
    • Sugumaran, M. (1991) Molecular mechanisms for mammalian melanogenesis. Comparison with insect cuticle sclerotization. FEBS Letters, 295, 233-239.
    • (1991) FEBS Letters , vol.295 , pp. 233-239
    • Sugumaran, M.1
  • 37
    • 0032524928 scopus 로고    scopus 로고
    • Laccase-and not tyrosinase-is the enzyme responsible for quinone methide production from 2,6-dimethoxy-4allyl phenol
    • Sugumara, M. and Bolton, J.L. (1998) Laccase-and not tyrosinase-is the enzyme responsible for quinone methide production from 2, 6-dimethoxy-4allyl phenol. Archives of Biochemistry and Biophysics, 15, 207-212.
    • (1998) Archives of Biochemistry and Biophysics , vol.15 , pp. 207-212
    • Sugumara, M.1    Bolton, J.L.2
  • 38
    • 0033113298 scopus 로고    scopus 로고
    • Insect melanogenesis. II. Inability of Manduca phenoloxidase to act on 5,6-dihydroxyindole-2-carboxylic acid
    • Sugumaran, M., Duggaraju, R., Generozova, F. and Ito, S. (1999) Insect melanogenesis. II. Inability of Manduca phenoloxidase to act on 5, 6-dihydroxyindole-2-carboxylic acid. Pigment Cell Research, 12, 118-125.
    • (1999) Pigment Cell Research , vol.12 , pp. 118-125
    • Sugumaran, M.1    Duggaraju, R.2    Generozova, F.3    Ito, S.4
  • 42
    • 79953143032 scopus 로고    scopus 로고
    • Melanization in living organisms: a perspective of species evolution
    • Vavricka, C.J., Christensen, B.M. and Li, J. (2010) Melanization in living organisms: a perspective of species evolution. Protein & Cell, 1, 830-841.
    • (2010) Protein & Cell , vol.1 , pp. 830-841
    • Vavricka, C.J.1    Christensen, B.M.2    Li, J.3
  • 43
    • 77954142798 scopus 로고    scopus 로고
    • Purification and N-glycosylation analysis of melanoma antigen dopachrome tautomerase
    • Vavricka, C.J., Ray, K.W., Christensen, B.M. and Li, J. (2010a) Purification and N-glycosylation analysis of melanoma antigen dopachrome tautomerase. Protein Journal, 29, 204-212.
    • (2010) Protein Journal , vol.29 , pp. 204-212
    • Vavricka, C.J.1    Ray, K.W.2    Christensen, B.M.3    Li, J.4
  • 44
    • 79551554500 scopus 로고    scopus 로고
    • From L-dopa to dihydroxyphenylacetaldehyde: A toxic biochemical pathway plays a vital physiological function in insects
    • Vavricka, C., Han, Q., Huang, Y., Erickson, S.M., Harich, K., Christensen, B.M. and Li, J. (2011) From L-dopa to dihydroxyphenylacetaldehyde: A toxic biochemical pathway plays a vital physiological function in insects. PLoS ONE, 6, e16124.
    • (2011) PLoS ONE , vol.6
    • Vavricka, C.1    Han, Q.2    Huang, Y.3    Erickson, S.M.4    Harich, K.5    Christensen, B.M.6    Li, J.7
  • 45
    • 0036299021 scopus 로고    scopus 로고
    • X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition
    • Wolf, E., De Angelis, J., Khalil, E.M., Cole, P.A. and Burley, S.K. (2002) X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition. Journal of Molecular Biology, 317, 215-224.
    • (2002) Journal of Molecular Biology , vol.317 , pp. 215-224
    • Wolf, E.1    De Angelis, J.2    Khalil, E.M.3    Cole, P.A.4    Burley, S.K.5
  • 46
    • 34547539768 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity of the reactive compounds generated in vitro by Manduca sexta phenoloxidase
    • Zhao, P., Li, J., Wang, Y. and Jiang, H. (2007) Broad-spectrum antimicrobial activity of the reactive compounds generated in vitro by Manduca sexta phenoloxidase. Insect Biochemistry and Molecular Biology, 37, 952-959.
    • (2007) Insect Biochemistry and Molecular Biology , vol.37 , pp. 952-959
    • Zhao, P.1    Li, J.2    Wang, Y.3    Jiang, H.4


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