Summary
Fluorescence decay kinetics of indole groups in five proteinases from microorganisms are reported. The data show differences between the excited state lifetimes of the tryptophans located in identical positions in the polypeptide chains of the closely related proteinases mesentericopeptidase and subtilisin Novo. The lifetime of the single Trp 113 in subtilisins DY and Carlsberg are identical. The microenvironments of this residue in the four subtilisins are identical and probably its fluorescence is quenched in these proteins. The crystallographic models of the enzymes investigated were analysed in the region of the tryptophyl residues and provide an explanation for the observed emission properties.
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© 1996 Plenum Press, New York
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Genov, N., Nikolov, P., Betzel, C., Wilson, K. (1996). Fluorescence Decay of Tryptophans in Serine Proteinases from Microorganisms: Relation to X-Ray Models. In: Bott, R., Betzel, C. (eds) Subtilisin Enzymes. Advances in Experimental Medicine and Biology, vol 379. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0319-0_15
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DOI: https://doi.org/10.1007/978-1-4613-0319-0_15
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