3.4.21.B55: pyrolysin

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For detailed information about pyrolysin, go to the full flat file.

Word Map on EC 3.4.21.B55

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 Hydrolases

3.4 Acting on peptide bonds (peptidases)

3.4.21 Serine endopeptidases

3.4.21.B55 pyrolysin

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Results	in table
1	AA Sequence
5	Cloned(Commentary)
4	General Stability
4	Inhibitors
2	kcat/KM [mM/s]
3	KM Value [mM]
5	Localization
4	Metals/Ions
5	Molecular Weight [Da]
2	Organic Solvent Stability
6	Organism
1	Oxidation Stability
4	pH Optimum
1	Posttranslational Modification
33	Protein Variants
5	Purification (Commentary)
1	Reaction
6	Reference
19	Substrates and Products (Substrate)
4	Subunits
5	Temperature Optimum [°C]
1	Temperature Range [°C]
12	Temperature Stability [°C]
3	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 3.4.21.B55 - pyrolysin

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proteolytic modification

Pyrococcus furiosus

P72186

the maturation of the enzyme involves autoprocessing of both the N-propeptide and a C-terminal propeptide. The long C-terminal extension can be dissected into a C-terminal propeptide and a C-terminal extension (CTEm) that is attached to the catalytic domain of the mature enzyme. Both of these propeptides assist in achieving pyrolysin hyperthermostability

721356