The role of tryptophan residues in the autoprocessing of prosubtilisin E

Sone, Michio; Falzon, Liliana; Inouye, Masayori

doi:10.1016/j.bbapap.2005.01.011

Cited by 8 publications

(12 citation statements)

References 33 publications

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“…This arrangement is similar to what is found in the prodomains of other serine proteases. In subtilisin E, a serine protease from Bacillus subtilis, the anti-parallel ␤-sheet in the propeptide is responsible for the stable interaction with two parallel helices in the subtilisin domain (38). In the complex, the prodomain is anchored to the surface of the molecule above the catalytic pocket of the enzyme and interacts mainly via the ␤-sheet surface (32), whereas the residues surrounding the BЈ/B site are extended to span the catalytic pocket.…”

Section: Discussionmentioning

confidence: 99%

Zymogen Activation and Subcellular Activity of Subtilisin Kexin Isozyme 1/Site 1 Protease

Palma

Burri

Oppliger

et al. 2014

Journal of Biological Chemistry

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Background: Zymogen activation of proprotein convertases requires excision of their prodomain for activity. Results: SKI-1/S1P matures into a plethora of forms that retain prodomain fragments and are active in different subcellular compartments. Conclusion: SKI-1/S1P appears as a unique proprotein convertase with an unusual mechanism of zymogen activation. Significance: Our study provides insights into how SKI-1/S1P matures and exerts its cellular activities, which is crucial for understanding its biological role.

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Section: Discussionmentioning

confidence: 99%

Zymogen Activation and Subcellular Activity of Subtilisin Kexin Isozyme 1/Site 1 Protease

Palma

Burri

Oppliger

et al. 2014

Journal of Biological Chemistry

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“…Trp106 and Trp113 are on one of the a-helices, and they play a significant role in fluorescence spectrum and subtilisin activity in subtilisin E [24]. In addition, W106Y, W113Y, and W106Y/ W113Y all show blue shifts in fluorescence spectra [24]. Therefore, mutation of Gly13 to Ala would cause the alteration of Trp106 and Trp113 that leads to a blue shift in fluorescence spectra.…”

Section: Discussionmentioning

confidence: 99%

“…Mutation to Ala would alter the interfacial interactions between the two domains, directly leading to the structural alterations of two a-helices of subtilisin domain. Trp106 and Trp113 are on one of the a-helices, and they play a significant role in fluorescence spectrum and subtilisin activity in subtilisin E [24]. In addition, W106Y, W113Y, and W106Y/ W113Y all show blue shifts in fluorescence spectra [24].…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, the alterations would lead to the alteration of Trp106 and Trp113. As studies on subtilisin E [24], G34A and G35A have a blue shift in fluorescence spectra.…”

Section: Essential Residues Of Nattokinase Propeptidementioning

confidence: 99%

“…As the study on subtilisin E [24], decrease in the a-helix content of subtilisin could be due to loosening of the secondary structure. However, G13A and G35A have increased helical contents that would lead to an altered structure of IMC.…”

Section: Essential Residues Of Nattokinase Propeptidementioning

confidence: 99%

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Four residues of propeptide are essential for precursor folding of nattokinase

Jia¹,

Cao²,

Deng³

et al. 2014

ABBS

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Subtilisin propeptide functions as an intramolecular chaperone that guides precursor folding. Nattokinase, a member of subtilisin family, is synthesized as a precursor consisting of a signal peptide, a propeptide, and a subtilisin domain, and the mechanism of its folding remains to be understood. In this study, the essential residues of nattokinase propeptide which contribute to precursor folding were determined. Deletion analysis showed that the conserved regions in propeptide were important for precursor folding. Single-site and multi-site mutagenesis studies confirmed the role of Tyr10, Gly13, Gly34, and Gly35. During stage (i) and (ii) of precursor folding, Tyr10 and Gly13 would form the part of interface with subtilisin domain. While Gly34 and Gly35 connected with an a-helix that would stabilize the structure of propeptide. The quadruple Ala mutation, Y10A/G13A/G34A/G35A, resulted in a loss of the chaperone function for the propeptide. This work showed the essential residues of propeptide for precursor folding via secondary structure and kinetic parameter analyses.

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Cold‐adapted maturation of thermophilic WF146 protease by mimicking the propeptide binding interactions of psychrophilic subtilisin S41

et al. 2008

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Thermophilic WF146 protease matures efficiently at 60°C, but quite slowly at low temperatures. In this report, seven amino acid residues involved in interactions between the mature domain and the propeptide of the enzyme were substituted by corresponding residues of psychrophilic subtilisin S41 to generate mutant Mut7 (S105G/G107D/Y117E/S136N/V143G/ K144E/D145S). Mut3 (S105G/G107D/Y117E) and Mut4 (S136N/V143G/K144E/D145S) were also constructed. Transferring structural features from S41 endowed Mut7 with a remarkably increased maturation rate, as well as an improved caseinolytic activity at 25°C. Moreover, Mut3 and Mut4 each obtained one of the above endowments. Further studies suggest that low-temperature activity and maturation rate are not necessarily linked, and uncoupling structural elements modulating the two properties may be advantageous to cold adaptation.

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The role of tryptophan residues in the autoprocessing of prosubtilisin E

Cited by 8 publications

References 33 publications

Zymogen Activation and Subcellular Activity of Subtilisin Kexin Isozyme 1/Site 1 Protease

Zymogen Activation and Subcellular Activity of Subtilisin Kexin Isozyme 1/Site 1 Protease

Four residues of propeptide are essential for precursor folding of nattokinase

Cold‐adapted maturation of thermophilic WF146 protease by mimicking the propeptide binding interactions of psychrophilic subtilisin S41

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