Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1969 Nov;100(2):935–938. doi: 10.1128/jb.100.2.935-938.1969

Effect of Inhibitors on Phenoloxidase of Mycobacterium leprae

K Prabhakaran 1, E B Harris 1, W F Kirchheimer 1
PMCID: PMC250177  PMID: 4982199

Abstract

Previous results had shown that the human leprosy bacilli possess a phenoloxidase, which, when compared with the enzyme from mammalian and plant sources, seemed unique in the range of substrates utilized and in the nature of the products formed. The effect of several inhibitors on the enzyme in Mycobacterium leprae was tested. Compounds which bind copper were found to be more effective than substrate analogues. Diethyldithiocarbamate penetrated the bacillus and completely suppressed its phenolase activity. Diasone (a derivative of diaminodiphenylsulfone used in the treatment of leprosy) proved to be a potent inhibitor of phenoloxidase of mammalian and plant origin. However, it was less efficient in the case of M. leprae. A biochemical peculiarity of M. leprae was observed in its ability to metabolize mimosine and penicillamine. These compounds produced total inhibition of tyrosinase in melanoma extract and of mushroom tyrosinase. Nontoxic inhibitors of phenoloxidase in the leprosy bacilli may be of value in developing a rational approach to chemotherapy of the disease.

Full text

PDF
935

Selected References

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

  1. Fowden L., Lewis D., Tristram H. Toxic amino acids: their action as antimetabolites. Adv Enzymol Relat Areas Mol Biol. 1967;29:89–163. doi: 10.1002/9780470122747.ch3. [DOI] [PubMed] [Google Scholar]
  2. Kirchheimer W. F., Prabhakaran K. Metabolic and biologic tests on mycobacteria once labeled as leprosy bacilli. Int J Lepr Other Mycobact Dis. 1968 Apr-Jun;36(2):162–165. [PubMed] [Google Scholar]
  3. LERNER A. B., FITZPATRICK T. B. Biochemistry of melanin formation. Physiol Rev. 1950 Jan;30(1):91–126. doi: 10.1152/physrev.1950.30.1.91. [DOI] [PubMed] [Google Scholar]
  4. MASON H. S. Comparative biochemistry of the phenolase complex. Adv Enzymol Relat Subj Biochem. 1955;16:105–184. doi: 10.1002/9780470122617.ch3. [DOI] [PubMed] [Google Scholar]
  5. Pirie A. Reaction of tyrosine oxidation products with proteins of the lens. Biochem J. 1968 Sep;109(2):301–305. doi: 10.1042/bj1090301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Prabhakaran K., Kirchheimer W. F., Harris E. B. Oxidation of phenolic compounds by Mycobacterium leprae and inhibition of phenolase by substrate analogues and copper chelators. J Bacteriol. 1968 Jun;95(6):2051–2053. doi: 10.1128/jb.95.6.2051-2053.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Prabhakaran K., Kirchheimer W. F. Use of 3,4-Dihydroxyphenylalanine Oxidation in the Identification of Mycobacterium leprae. J Bacteriol. 1966 Oct;92(4):1267–1268. doi: 10.1128/jb.92.4.1267-1268.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Prabhakaran K. Oxidation of 3,4-dihydroxyphenylalanine (DOPA) by Mycobacterium leprae. Int J Lepr Other Mycobact Dis. 1967 Jan-Mar;35(1):42–51. [PubMed] [Google Scholar]
  9. Prabhakaran K. Phenoloxidase of Mycobacterium leprae. Nature. 1967 Jul 22;215(5099):436–437. doi: 10.1038/215436a0. [DOI] [PubMed] [Google Scholar]
  10. Smith H. Biochemical challenge of microbial pathogenicity. Bacteriol Rev. 1968 Sep;32(3):164–184. doi: 10.1128/br.32.3.164-184.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. WOSILAIT W. D., NASON A. Pyridine nucleotide-quinone reductase. I. Purification and properties of the enzyme from pea seeds. J Biol Chem. 1954 Jan;206(1):255–270. [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES