3.4.21.B55: pyrolysin
This is an abbreviated version!
For detailed information about pyrolysin, go to the full flat file.
Word Map on EC 3.4.21.B55
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3.4.21.B55
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hyperthermophilic
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pyrococcus
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furiosus
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subtilisin-like
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subtilases
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archaeon
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hyperthermostable
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n-glycosylation
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asn
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autoproteolysis
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subtilisin
- 3.4.21.B55
-
hyperthermophilic
-
pyrococcus
- furiosus
-
subtilisin-like
-
subtilases
- archaeon
-
hyperthermostable
-
n-glycosylation
- asn
-
autoproteolysis
- subtilisin
Reaction
endopeptidase with two preferential cleavage sites in alphaS1-casein, at bonds Gln9-/-Gly10 and Leu16-/-Asn17 =
ECTree
3.4.21.B55 pyrolysinAdvanced search results
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results (General Stability
General Stability on EC 3.4.21.B55 - pyrolysin
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GENERAL STABILITY 
ORGANISM
UNIPROT
LITERATURE
binding of Ca2+ increases the stability of the PPC domain and, in turn, stabilizes the global structure of the enzyme by modulating interdomain interactions
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four inserts in the catalytic domain of hyperthermostable pyrolysin contribute to the folding, maturation, stability, and activity of the enzyme at high temperatures. The modification of extra structural elements in pyrolysin-like proteases is a promising strategy for modulating global structure stability and enzymatic activity of this class of protease
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supplementation of Na+, Ca2+, or Mg2+ salts at concentrations similar to those in seawater destabilizes recombinant pyrolysin. Ca2+ and Mg2+ are stronger denaturants than Na+ for pyrolysin. Ca2+ also acts a stabilizer of pyrolysin by binding to the enzyme at specific sites. The destabilizing effect of metal ions on pyrolysin appears to be related to the disturbance of surface electrostatic interactions of the enzyme
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