(Q47798521)

English

Purification and biochemical analysis of WprA, a 52-kDa serine protease secreted by B. subtilis as an active complex with its 23-kDa propeptide

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scholarly article

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

Purification and biochemical analysis of WprA, a 52-kDa serine protease secreted by B. subtilis as an active complex with its 23-kDa propeptide (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

author name string

L M Babé

1

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

B Schmidt

2

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

publication date

1 July 1998

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

Biochimica et Biophysica Acta

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

1386

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

1

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

211-219

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

Secretion, processing and activation of bacterial extracellular proteases

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Multiple active forms of a novel serine protease from Bacillus subtilis

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Cloning and characterization of the gene for an additional extracellular serine protease of Bacillus subtilis

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Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases

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The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease

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Recruitment of substrate-specificity properties from one enzyme into a related one by protein engineering

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Engineering a Bacillus subtilis expression-secretion system with a strain deficient in six extracellular proteases

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Cloning, sequencing, and secretion of Bacillusamyloliquefacienssubtillisin inBacillus subtilis

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Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis

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Controlled proteolysis of tubulin by subtilisin: localization of the site for MAP2 interaction.

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Interaction of subtilisin BPN' and recombinant Streptomyces subtilisin inhibitors with substituted P1 site residues.

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Ionizable P1 residues in serine proteinase inhibitors undergo large pK shifts on complex formation.

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On the size of the active site in proteases. I. Papain

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Identifiers

10.1016/S0167-4838(98)00110-1

0 references

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9675284

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