3.4.21.B54: Pyrococcus abyssi serine endopeptidase

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For detailed information about Pyrococcus abyssi serine endopeptidase, go to the full flat file.

Reaction

high affinity for aromatic (Phe and Tyr) and hydrophobic amino acids (mainly Leu) in P1 position, specificity for aromatic moieties in P1' position =

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.B54 Pyrococcus abyssi serine endopeptidase

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Results	in table
1	General Stability
8	Inhibitors
1	Molecular Weight [Da]
2	Organism
1	pH Optimum
1	pH Range
1	Purification (Commentary)
1	Reaction
2	Reference
6	Substrates and Products (Substrate)
2	Subunits
1	Temperature Optimum [°C]
1	Temperature Range [°C]
4	Temperature Stability [°C]

Subunits

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Subunits on EC 3.4.21.B54 - Pyrococcus abyssi serine endopeptidase

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

oligomer

2 entries

oligomer

Pyrococcus abyssi

-

x * 18800, PfPI protease has a monomeric form of 18800 Da oligomerising into a form of 200000 Da. The monomer and dimer are proteolyticaly inactive, SDS-PAGE

722254

oligomer

Pyrococcus abyssi st 549

-

x * 18800, PfPI protease has a monomeric form of 18800 Da oligomerising into a form of 200000 Da. The monomer and dimer are proteolyticaly inactive, SDS-PAGE

-