Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin

Zhixiang Hu, Khadijeh Haghjoo, Frank Jordan

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Evidence is presented for some secondary structure, very likely α- helical, of the propeptide of subtilisin E in aqueous salt solution, as well as for strong intermolecular interactions between the propeptide and the mature sequence both in the processed and unprocessed states (i.e. in prosubtilisin). Prosubtilisin is shown to exist as a dimer according to size exclusion high performance liquid chromatography under nondenaturing conditions; that dimer may be on the autoprocessing pathway. According to such a model, the prosequence of one prosubtilisin molecule is the template for the refolding of the mature sequence of the second, and, in turn, the hydrolytic process is intermolecular as well. Support for such an intermolecular folding model also includes potent slow binding inhibition of subtilisin by the propeptide, specific proteolysis of the propeptide by subtilisin, and evidence for intermolecular processing under a variety of conditions.

Original languageEnglish (US)
Pages (from-to)3375-3384
Number of pages10
JournalJournal of Biological Chemistry
Volume271
Issue number7
DOIs
StatePublished - Feb 16 1996

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Subtilisin
Dimers
Proteolysis
Subtilisins
Enzyme inhibition
High performance liquid chromatography
Salts
High Pressure Liquid Chromatography
Molecules
Processing
prosubtilisin

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "Evidence is presented for some secondary structure, very likely α- helical, of the propeptide of subtilisin E in aqueous salt solution, as well as for strong intermolecular interactions between the propeptide and the mature sequence both in the processed and unprocessed states (i.e. in prosubtilisin). Prosubtilisin is shown to exist as a dimer according to size exclusion high performance liquid chromatography under nondenaturing conditions; that dimer may be on the autoprocessing pathway. According to such a model, the prosequence of one prosubtilisin molecule is the template for the refolding of the mature sequence of the second, and, in turn, the hydrolytic process is intermolecular as well. Support for such an intermolecular folding model also includes potent slow binding inhibition of subtilisin by the propeptide, specific proteolysis of the propeptide by subtilisin, and evidence for intermolecular processing under a variety of conditions.",
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Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin. / Hu, Zhixiang; Haghjoo, Khadijeh; Jordan, Frank.

In: Journal of Biological Chemistry, Vol. 271, No. 7, 16.02.1996, p. 3375-3384.

Research output: Contribution to journalArticle

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AB - Evidence is presented for some secondary structure, very likely α- helical, of the propeptide of subtilisin E in aqueous salt solution, as well as for strong intermolecular interactions between the propeptide and the mature sequence both in the processed and unprocessed states (i.e. in prosubtilisin). Prosubtilisin is shown to exist as a dimer according to size exclusion high performance liquid chromatography under nondenaturing conditions; that dimer may be on the autoprocessing pathway. According to such a model, the prosequence of one prosubtilisin molecule is the template for the refolding of the mature sequence of the second, and, in turn, the hydrolytic process is intermolecular as well. Support for such an intermolecular folding model also includes potent slow binding inhibition of subtilisin by the propeptide, specific proteolysis of the propeptide by subtilisin, and evidence for intermolecular processing under a variety of conditions.

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