Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1981 Jul;147(1):69–74. doi: 10.1128/jb.147.1.69-74.1981

Stimulation of bacterial arylsulfatase activity by arylamines: evidence for substrate activation.

J R George, J W Fitzgerald
PMCID: PMC216008  PMID: 7240096

Abstract

A number of arylamines (including tyramine and tryptamine) increased the in vitro activity of arylsulfatase from Pseudomonas sp. strain C12B. Amino acid analogs of these amines (e.g., tyrosine and tryptophan) failed to exert an effect. Stimulation of activity by tyramine could not be accounted for in terms of sulfotransferase activity for this phenol, and no shift in the pH optimum for the enzyme occurred in the presence of tryptamine. Increased Vmax due to these amines was independent of enzyme concentration but varied significantly with substrate concentration. Evidence is presented which suggests that arylamines enhance arylsulfatase activity by forming a salt linkage with the substrate and rendering it more susceptible to enzymatic and acid-catalyzed hydrolyses. The recrystallized tryptamine salt of the substrate exhibited a reduced affinity for the enzyme but was hydrolyzed more rapidly than the potassium salt, which is normally employed as the assay substrate.

Full text

PDF
69

Selected References

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

  1. Adachi T., Murooka Y., Harada T. Derepression of arylsulfatase synthesis in Aerobacter aerogenes by tyramine. J Bacteriol. 1973 Oct;116(1):19–24. doi: 10.1128/jb.116.1.19-24.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bartholomew B., Dodgson K. S., Matcham G. W., Shaw D. J., White G. F. A novel mechanism of enzymic ester hydrolysis. Inversion of configuration and carbon-oxygen bond cleavage by secondary alkylsulphohydrolases from detergent-degrading micro-organisms. Biochem J. 1977 Sep 1;165(3):575–580. doi: 10.1042/bj1650575. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Burns G. R., Galanopoulou E., Wynn C. H. Kinetic studies of the phenol sulphate-phenol sulphotransferase of Aspergillus oryzae. Biochem J. 1977 Oct 1;167(1):223–227. doi: 10.1042/bj1670223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Burns G. R., Wynn C. H. A rapid direct assay for the determination of the separate activities of the three arylsulphatases of Aspergillus oryzae. Biochem J. 1977 Sep 15;166(3):411–413. doi: 10.1042/bj1660411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Burns G. R., Wynn C. H. Studies on the Arylsulphatase and phenol sulphotransferase activities of Aspergillus oryzae. Biochem J. 1975 Sep;149(3):697–705. doi: 10.1042/bj1490697. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cloves J. M., Dodgson K. S., Games D. E., Shaw D. J., White G. F. The mechanism of action of primary alkylsulphohydrolase and arylsulphohydrolase from a detergent-degrading micro-organism. Biochem J. 1977 Dec 1;167(3):843–846. doi: 10.1042/bj1670843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. DODGSON K. S. Determination of inorganic sulphate in studies on the enzymic and non-enzymic hydrolysis of carbohydrate and other sulphate esters. Biochem J. 1961 Feb;78:312–319. doi: 10.1042/bj0780312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. DODGSON K. S. Observations on the arylsulphatase of Proteus vulgaris. Enzymologia. 1959 Jul 15;20:301–312. [PubMed] [Google Scholar]
  9. DODGSON K. S., POWELL G. M. Studies on sulphatases. 26. Arylsulphatase activity in the digestive juice and digestive gland of Helix pomatia. Biochem J. 1959 Dec;73:666–671. doi: 10.1042/bj0730666. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. DODGSON K. S., ROSE F. A., SPENCER B. Studies on sulphatases. 10. The isolation and characterization of biosynthetic arylsulphates. Biochem J. 1955 Jun;60(2):346–352. doi: 10.1042/bj0600346. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Delisle G. J., Milazzo F. H. Characterization of arylsulfatase isoenzymes from Pseudomonas aeruginosa. Can J Microbiol. 1972 May;18(5):561–568. doi: 10.1139/m72-089. [DOI] [PubMed] [Google Scholar]
  12. Delisle G., Milazzo F. H. The isolation of arylsulphatase isoenzymes from Pseudomonas aeruginosa. Biochim Biophys Acta. 1970 Sep 16;212(3):505–508. doi: 10.1016/0005-2744(70)90258-5. [DOI] [PubMed] [Google Scholar]
  13. FOWLER L. R., RAMMLER D. H. SULFUR METABOLISM OF AEROBACTOR AEROGENES. II. THE PURIFICATION AND SOME PROPERTIES OF A SULFATASE. Biochemistry. 1964 Feb;3:230–237. doi: 10.1021/bi00890a015. [DOI] [PubMed] [Google Scholar]
  14. Farooqui A. A. Sulfatases, sulfate esters and their metabolic disorders. Clin Chim Acta. 1980 Jan 31;100(3):285–299. doi: 10.1016/0009-8981(80)90278-8. [DOI] [PubMed] [Google Scholar]
  15. Fitzgerald J. W., Kight L. C. Physiological control of alkylsulfatase synthesis in Pseudomonas aeruginosa: effects of glucose, glucose analogs, and sulfur. Can J Microbiol. 1977 Oct;23(10):1456–1464. doi: 10.1139/m77-214. [DOI] [PubMed] [Google Scholar]
  16. Fitzgerald J. W. Sulfate ester formation and hydrolysis: a potentially important yet often ignored aspect of the sulfur cycle of aerobic soils. Bacteriol Rev. 1976 Sep;40(3):698–721. doi: 10.1128/br.40.3.698-721.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. George J. R., Fitzgerald J. W. Arylsulfatase from Pseudomonas sp. strain C12B: purification to homogeneity, immunological analysis, and physical properties. J Bacteriol. 1981 Mar;145(3):1428–1431. doi: 10.1128/jb.145.3.1428-1431.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Henderson M. J., Milazzo F. H. Arylsulfatase in Salmonella typhimurium: detection and influence of carbon source and tyramine on its synthesis. J Bacteriol. 1979 Jul;139(1):80–87. doi: 10.1128/jb.139.1.80-87.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Murooka Y., Yamada T., Tanabe S., Harada T. Immunological study of the regulation of cellular arylsulfatase synthesis in Klebsiella aerogenes. J Bacteriol. 1977 Oct;132(1):247–253. doi: 10.1128/jb.132.1.247-253.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Murooka Y., Yim M. H., Harada T. Formation and Purification of Serratia marcescens Arylsulfatase. Appl Environ Microbiol. 1980 Apr;39(4):812–817. doi: 10.1128/aem.39.4.812-817.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Oka M., Murooka Y., Harada T. Genetic control of tyramine oxidase, which is involved in derepressed synthesis of arylsulfatase in Klebsiella aerogenes. J Bacteriol. 1980 Jul;143(1):321–327. doi: 10.1128/jb.143.1.321-327.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Roy A. B. L-ascorbic acid 2-sulphate. A substrate for mammalian arylsulphatases. Biochim Biophys Acta. 1975 Feb 19;377(2):356–363. doi: 10.1016/0005-2744(75)90316-2. [DOI] [PubMed] [Google Scholar]
  23. SPENCER B. Studies on sulphatases. 20. Enzymic cleavage of aryl hydrogen sulphates in the presence of H218O. Biochem J. 1958 May;69(1):155–159. doi: 10.1042/bj0690155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. STEINER R. F., LIPPOLDT R. E., EDELHOCH H., FRATTALI V. ULTRAVIOLET FLUORESCENCE OF PROTEINS: INFLUENCE OF CONFORMATION AND ENVIRONMENT. Biopolym Symp. 1964;13:355–366. [PubMed] [Google Scholar]
  25. Suh N. N., Ebringer A. Continuous distribution of quantitative antibody responses to strain C3000 Escherichia coli in inbred mice [proceedings]. Biochem Soc Trans. 1979 Feb;7(1):188–191. doi: 10.1042/bst0070188. [DOI] [PubMed] [Google Scholar]

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

RESOURCES