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Molecular and Cellular Biochemistry

, Volume 60, Issue 2, pp 109–114 | Cite as

Biotin analogs activate guanylate cyclase

  • David L. Vesely
  • Henry C. Wormser
  • Hanley N. bramson
Original Articles

Summary

The sulfur atom in the vitamin biotin has previously been suggested to be essential in biotin's mechanism of action. In a series of investigations on structure-function relationships with biotin analogs not containing the sulfur atom, the biotin analogs, azabiotin, bisnorazabiotin, carbobiotin and isoazabiotin enhanced guanylate cyclase, an enzyme that has recently been demonstrated to be activated by biotin. These analogs increased guanylate cyclase activity two-fold in liver, cerebellum, heart, kidney and colon at 1 μM concentrations. The ED50 for stimulation of guanulate cyclase activity occurred at 0.1 μM for each of the biotin analogs. These data indicate that the sulfur atom is not essential in biotin's activation of guanylate cyclase since these analogs do not contain the sulfur atom. Studies on the ring structure of biotin revealed that even compounds with a single 5-membered ring (2-imidazolidone) could augment guanylate cyclase activity. The guanylate cyclase co-factor manganese was not essential for the enhancement of guanylate cyclase by these agents but a maximal activation of this enzyme by these analogs could not be obtained without manganese present.

Keywords

Sulfur Manganese Biotin Maximal Activation Sulfur Atom 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Martinus Niihoff Publishers 1984

Authors and Affiliations

  • David L. Vesely
    • 1
    • 2
  • Henry C. Wormser
    • 1
    • 2
  • Hanley N. bramson
    • 1
    • 2
  1. 1.Department of MedicineUniversity of Arkansas for Medical SciencesLittle RockUSA
  2. 2.College of Pharmacy and Allied Health ProfessionsWayne State UniversityDetroit.USA

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