Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1984 Sep 1;222(2):407–411. doi: 10.1042/bj2220407

Oxidation of tyrosine residues in proteins by tyrosinase. Formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine.

S Ito, T Kato, K Shinpo, K Fujita
PMCID: PMC1144193  PMID: 6433900

Abstract

A simple and rapid method was developed for the determination of 3,4-dihydroxyphenylalanine (dopa) and 5-S-cysteinyl-3,4-dihydroxyphenylalanine (5-S-cysteinyldopa) in proteins with the use of high-pressure liquid chromatography. With this method, it is demonstrated that mushroom tyrosinase can catalyse hydroxylation of tyrosine residues in proteins to dopa and subsequent oxidation to dopaquinone residues. The dopaquinone residues in proteins combine with cysteine residues to form 5-S-cysteinyldopa in bovine serum albumin and yeast alcohol dehydrogenase, whereas dopa is the major product in bovine insulin, which lacks cysteine residues.

Full text

PDF
407

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Agrup G., Hansson C., Rorsman H., Rosengren A. M., Rosengren E. 5-S-cysteinyldopa and trichochromes in red feathers. Acta Derm Venereol. 1978;58(3):269–270. [PubMed] [Google Scholar]
  2. Agrup G., Hansson C., Rorsman H., Rosengren A. M., Rosengren E. Free and bound 5-S-cysteinyldopa and dopa in human malignant melanomas. Acta Derm Venereol. 1978;58(3):270–272. [PubMed] [Google Scholar]
  3. Agrup G., Hansson C., Rorsman H., Rosengren E. The effect of cysteine on oxidation of tyrosine, dopa, and cysteinyldopas. Arch Dermatol Res. 1982;272(1-2):103–115. doi: 10.1007/BF00510400. [DOI] [PubMed] [Google Scholar]
  4. Cory J. G., Frieden E. Differential reactivities of tyrosine residues of proteins to tyrosinase. Biochemistry. 1967 Jan;6(1):121–126. doi: 10.1021/bi00853a021. [DOI] [PubMed] [Google Scholar]
  5. Cory J. G., Frieden E. Faster oxidation of tyrosine-26 of oxidized b chain of insulin by tyrosinase. Biochemistry. 1967 Jan;6(1):116–120. doi: 10.1021/bi00853a020. [DOI] [PubMed] [Google Scholar]
  6. Hearing V. J., Jr, Ekel T. M., Montague P. M., Nicholson J. M. Mammalin tyrosinase. Stoichiometry and measurement of reaction products. Biochim Biophys Acta. 1980 Feb 14;611(2):251–268. doi: 10.1016/0005-2744(80)90061-3. [DOI] [PubMed] [Google Scholar]
  7. Ito S., Homma K., Kiyota M., Fujita K., Jimbow K. Characterization of structural properties for morphologic differentiation of melanosomes. III. free and protein-bound dopa and 5-S-cysteinyldopa in B16 and Harding-Passey melanomas. J Invest Dermatol. 1983 Mar;80(3):207–209. doi: 10.1111/1523-1747.ep12534160. [DOI] [PubMed] [Google Scholar]
  8. Ito S., Inoue S., Yamamoto Y., Fujita K. Synthesis and antitumor activity of cysteinyl-3,4-dihydroxyphenylalanines and related compounds. J Med Chem. 1981 Jun;24(6):673–677. doi: 10.1021/jm00138a006. [DOI] [PubMed] [Google Scholar]
  9. Ito S., Jimbow K., Kato T., Kiyota M., Fujita K. Protein-bound dopa and 5-S-cysteinyldopa in non-melanogenic tissues. Acta Derm Venereol. 1983;63(6):463–467. [PubMed] [Google Scholar]
  10. Ito S., Prota G. A facile one-step synthesis of cysteinyldopas using mushroom tyrosinase. Experientia. 1977 Aug 15;33(8):1118–1119. doi: 10.1007/BF01946005. [DOI] [PubMed] [Google Scholar]
  11. Jimbow K., Quevedo W. C., Jr, Fitzpatrick T. B., Szabo G. Some aspects of melanin biology: 1950-1975. J Invest Dermatol. 1976 Jul;67(1):72–89. doi: 10.1111/1523-1747.ep12512500. [DOI] [PubMed] [Google Scholar]
  12. Prota G. Recent advances in the chemistry of melanogenesis in mammals. J Invest Dermatol. 1980 Jul;75(1):122–127. doi: 10.1111/1523-1747.ep12521344. [DOI] [PubMed] [Google Scholar]
  13. Takahashi H., Fitzpatrick T. B. Large amounts of deoxyphenylalanine in the hydrolysate of melanosomes from Harding-Passey mouse melanoma. Nature. 1966 Feb 26;209(5026):888–890. doi: 10.1038/209888a0. [DOI] [PubMed] [Google Scholar]
  14. Tse D. C., McCreery R. L., Adams R. N. Potential oxidative pathways of brain catecholamines. J Med Chem. 1976 Jan;19(1):37–40. doi: 10.1021/jm00223a008. [DOI] [PubMed] [Google Scholar]
  15. Waite J. H. Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis L. J Biol Chem. 1983 Mar 10;258(5):2911–2915. [PubMed] [Google Scholar]
  16. YASUNOBU K. T., PETERSON E. W., MASON H. S. The oxidation of tyrosine-containin peptides by tyrosinase. J Biol Chem. 1959 Dec;234:3291–3295. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES