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Literature summary for 3.4.21.B56 extracted from

  • Yokoyama, H.; Matsui, I.
    A novel thermostable membrane protease forming an operon with a stomatin homolog from the hyperthermophilic archaebacterium Pyrococcus horikoshii (2005), J. Biol. Chem., 280, 6588-6594.
    View publication on PubMed
Search for more literature for 3.4.21.B56

Cloned(Commentary)

Cloned (Comment) Organism
the N-terminal region of PH1510 (1510-N, residues 16–236) is expressed in Escherichia coli Pyrococcus horikoshii

Protein Variants

Protein Variants Comment Organism
D168A mutant enzyme shows 3.2% activity with casein compared with the activity of the wild-type enzyme. The mutant enzyme shows a 25000 Da band instead of 45000 Da band Pyrococcus horikoshii
K138A mutant enzyme shows 1.2% activity with casein compared with the activity of the wild-type enzyme Pyrococcus horikoshii
S97A mutant enzyme shows 0.08% activity with casein compared with the activity of the wild-type enzyme Pyrococcus horikoshii
T62A mutant enzyme shows 5.5% activity with casein compared with the activity of the wild-type enzyme Pyrococcus horikoshii

Inhibitors

Inhibitors Comment Organism Structure
3,4-dichloroisocoumarin 1 mM, 49% inhibition Pyrococcus horikoshii
CaCl2 0.1 M, 11% activity Pyrococcus horikoshii
dodecyl-beta-D-maltoside 0.1%, 38% activity Pyrococcus horikoshii
EDTA 5 mM, 67% inhibition Pyrococcus horikoshii
iodoacetate 5 mM, 17% inhibition Pyrococcus horikoshii
MgCl2 0.1 M, 14% residual activity Pyrococcus horikoshii
MnCl2 0.1 M, 4% activity Pyrococcus horikoshii
NaCl 0.1 M, 90% loss of activity Pyrococcus horikoshii
pepstatin 0.005 mM, 21% inhibition Pyrococcus horikoshii
phenylmethylsulfonyl fluoride 5 mM, 21% inhibition Pyrococcus horikoshii
SDS 0.01%, 53% activity. 1% SDS, 1.2% activity Pyrococcus horikoshii
ZnCl2 0.1 M, 9% activity Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
 2 * 25000, dimer of the N-terminal fragment of PH1510 (1510-N, residues 16–236), SDS-PAGE Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O59179 N-terminal region of open reading frame, PH1510 (residues 16–236, designated as 1510-N) is a serine protease
-

Purification (Commentary)

Purification (Comment) Organism
purification of the N-terminal fragment of PH1510 (1510-N, residues 16–236) expressed in Escherichia coli Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein + H2O alpha-casein is not cleaved as effectively as beta-casein. 1510-N probably cleaves the substrate specifically. The cleavage sites contain many hydrophobic and aromatic residues. The 1510-N protease possibly recognizes leucine at the cleavage site Pyrococcus horikoshii ?
-
 ?
beta-casein + H2O alpha-casein is not cleaved as effectively as beta-casein. 1510-N probably cleaves the substrate specifically. The cleavage sites contain many hydrophobic and aromatic residues. The 1510-N protease possibly recognizes leucine at the cleavage site Pyrococcus horikoshii ?
-
 ?
additional information 1510-N is a serine protease with a catalytic residue, Ser-97 Pyrococcus horikoshii ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 25000, dimer of the N-terminal fragment of PH1510 (1510-N, residues 16–236), SDS-PAGE Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
PH1510
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
 assay at Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 6
-
 Pyrococcus horikoshii