Proceedings of the Indian Academy of Sciences - Chemical Sciences

, Volume 93, Issue 8, pp 1289–1304

Chemical probes into the active centre of a heme thiolate monoxygenase

Authors

  • P K Bhattacharyya
    • Department of BiochemistryUniversity of Illinois
    • Department of Organic ChemistryIndian Institute of Science
  • T B Samanta
    • Department of BiochemistryUniversity of Illinois
  • A H J Ullah
    • Department of BiochemistryUniversity of Illinois
  • I C Gunsalus
    • Department of BiochemistryUniversity of Illinois
Organic

DOI: 10.1007/BF02869936

Cite this article as:
Bhattacharyya, P.K., Samanta, T.B., Ullah, A.H.J. et al. Proc. Indian Acad. Sci. (Chem. Sci.) (1984) 93: 1289. doi:10.1007/BF02869936
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Abstract

Linalool-8-monoxygenase, a typical bacterial P-450 heme thiolase, shows a high degree of substrate specificity towards linalool. The active site of the pure enzyme has been probed with a large number of substrate analogues with systematic alterations or conformational variations in the linalool molecule. The comparison of three parameters, the mo→mos conversion of the enzyme as a result of substrate binding monitored at 392 nm, theKD of the analogues giving information about energies of association and the relative turnover as substrate have given information about the space-filling characteristics of the substrates in the enzyme cleft, the number of contacts the molecules make with the respective domains of the enzyme and the distance of the site undergoing hydroxylation from the oxygen site, respectively. The data permit the conclusion that linalool makes contact with the enzyme by hydrogen bonding with the hydroxyl group as well through hydrophobic association with all the eight carbons carrying hydrogen in the molecules.

Keywords

EnzymesoxygenasesP-450 hydroxylasesstructure of monooxygenasesubstrate analoguesenzyme kineticsintermolecular associations
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© Indian Academy of Sciences 1984