3.4.21.B56: Pyrococcus horikoshii membrane protease PH1510
This is an abbreviated version!
For detailed information about Pyrococcus horikoshii membrane protease PH1510, go to the full flat file.
Word Map on EC 3.4.21.B56
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3.4.21.B56
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hyperthermophilic
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archaeon
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dyad
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hemolytic
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anemia
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stomatocytosis
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ser-lys
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erythrocyte
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superposition
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coiled-coil
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symmetry-related
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ob-fold
- 3.4.21.B56
-
hyperthermophilic
- archaeon
-
dyad
-
hemolytic
-
anemia
-
stomatocytosis
- ser-lys
- erythrocyte
-
superposition
-
coiled-coil
-
symmetry-related
-
ob-fold
Reaction
Synonyms
1510-C, 1510-N, membrane stomatin-specific protease, PH1510, PH1510p, stomatin operon partner protein, Stomatin/STOPP, STOPP, STOPP PH1510
ECTree
3.4.21.B56 Pyrococcus horikoshii membrane protease PH1510Advanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.B56 - Pyrococcus horikoshii membrane protease PH1510
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
?
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
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-
?
p-stomatin PH1511 + H2O
?
the N-terminal region of PH1510 (residues 16-236, i.e. 1510-N) is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138) and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511
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-
?
p-stomatin PH1511p + H2O
?
the N-terminal region of PH1510p is a serine protease and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p
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-
?
stomatin-homolog PH1511 + H2O
?
the N-terminal region of an open reading frame, PH1510 (residues 16236, designated as 1510-N) is a serine protease with a catalytic Ser-Lys dyad that specifically cleaves the C-terminal hydrophobic residues of a membrane protein, the stomatin-homolog PH1511
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-
?
stomatin-homolog PH1511 + H2O
?
the N-terminal region of an open reading frame, PH1510 (residues 16236, designated as 1510-N) is a serine protease with a catalytic Ser-Lys dyad that specifically cleaves the C-terminal hydrophobic residues of a membrane protein, the stomatin-homolog PH1511
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-
?
additional information
?
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1510-N is a serine protease with a catalytic residue, Ser-97
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-
?
additional information
?
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1510-N is a serine protease with a catalytic residue, Ser-97
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-
?
additional information
?
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binding of the substrate to the catalytic site of 1510-N induces conformational changes in a region that includes loop L2 so that Lys138 approaches the catalytic Ser97
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-
?
additional information
?
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binding of the substrate to the catalytic site of 1510-N induces conformational changes in a region that includes loop L2 so that Lys138 approaches the catalytic Ser97
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-
?
additional information
?
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peptide substrate binding structure of the enzyme, detailed analysis and overview. The six central residues, VIVLML, of the peptide are hydrophobic and in a pseudopalindromic structure and therefore favorably fit into the hydrophobic active tunnel of the enzyme dimer, although the enzyme degrades the substrate at only one point. Binding of the substrate causes a large rotational and translational displacement between protomers and produces a tunnel suitable for binding the peptide. When the peptide binds, the flexible L2 loop of one protomer forms beta-strands, whereas that of the other protomer remains in a loop form, indicating that one protomer binds to the peptide more tightly than the other protomer. The Ala138 residues of the two protomers are located very close together, close positioning of the catalytic Ser97 and Lys138 residues may be induced by electrostatic repulsion of the two Lys138 side chains of the protomers
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-
?
additional information
?
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-
peptide substrate binding structure of the enzyme, detailed analysis and overview. The six central residues, VIVLML, of the peptide are hydrophobic and in a pseudopalindromic structure and therefore favorably fit into the hydrophobic active tunnel of the enzyme dimer, although the enzyme degrades the substrate at only one point. Binding of the substrate causes a large rotational and translational displacement between protomers and produces a tunnel suitable for binding the peptide. When the peptide binds, the flexible L2 loop of one protomer forms beta-strands, whereas that of the other protomer remains in a loop form, indicating that one protomer binds to the peptide more tightly than the other protomer. The Ala138 residues of the two protomers are located very close together, close positioning of the catalytic Ser97 and Lys138 residues may be induced by electrostatic repulsion of the two Lys138 side chains of the protomers
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-
?
additional information
?
-
binding of the substrate to the catalytic site of 1510-N induces conformational changes in a region that includes loop L2 so that Lys138 approaches the catalytic Ser97
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-
?
