Abstract
Thermitase (EC 3.4.21.14) is an extracellular thermostable serine proteinase isolated from Thermoactinomyces vulgaris culture filtrate [1–3]. The enzyme resembles in its characteristics the subtilisins. This is strongly indicated especially by the structure of the active site peptide [4]. The enzyme contains one methionine and one cysteine residue; these two residues are apparently functionally important [4]. Closely related seem to be the alkaline proteinases of Bacillus cereus and Bacillus thuringiensis [5] and proteinase K from the mold Tritirachium album [6]. Our interest in structural investigation of thermitase was stimulated by the problem of its apparently essential cysteinyl residue, by the lack of information on evolutionary relations between thermitase and other subtilisin-type enzymes and on the structural basis of the increased thermostability of thermitase. Another factor not to be neglected was the practical importance of the enzyme. Since the localization of the methionine residue was known from one of the early studies we decided to start our sequence work with the cyanogen bromide digest of the enzyme.
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Baudyš, M., Meloun, B., Kostka, V., Hausdorf, G., Frömmel, C., Höhne, W.E. (1987). Structure of Thermitase, A Thermostable Serine Proteinase from Thermoactinomyces Vulgaris, and its Relationship with Subtilisin-Type Proteinases. In: Chaloupka, J., Krumphanzl, V. (eds) Extracellular Enzymes of Microorganisms. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1274-1_8
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DOI: https://doi.org/10.1007/978-1-4684-1274-1_8
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