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Information on EC 3.4.21.B56 - Pyrococcus horikoshii membrane protease PH1510
for references in articles please use BRENDA:EC3.4.21.B56
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Please check here for current data: EC unknown
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.B56 Pyrococcus horikoshii membrane protease PH1510
The expected taxonomic range for this enzyme is: Pyrococcus horikoshii
- 3.4.21.B56
-
hyperthermophilic
- archaeon
-
dyad
-
hemolytic
-
anemia
-
stomatocytosis
- ser-lys
- erythrocyte
-
superposition
-
coiled-coil
-
symmetry-related
-
ob-fold
Synonyms
1510-n, ph1510, 1510-c, ph1510p, stopp ph1510, stomatin operon partner protein, stomatin/stopp, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1510-N
PH1510
1510-N
N-terminal region of open reading frame, PH1510 (residues 16236, designated as 1510-N)
1510-N
N-terminal region of open reading frame, PH1510 (residues 16236, designated as 1510-N)
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-casein + H2O
?
Substrates: 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
Products: -
Products: -
?
beta-casein + H2O
?
Substrates: 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
Products: -
Products: -
?
p-stomatin PH1511 + H2O
?
Substrates: 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
Products: -
Products: -
?
p-stomatin PH1511p + H2O
?
Substrates: the N-terminal region of PH1510p is a serine protease and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p
Products: -
Products: -
?
stomatin-homolog PH1511 + H2O
?
Substrates: 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
Products: -
Products: -
?
stomatin-homolog PH1511 + H2O
?
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 1510-N is a serine protease with a catalytic residue, Ser-97
Products: -
Products: -
?
additional information
?
-
-
Substrates: 1510-N is a serine protease with a catalytic residue, Ser-97
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
p-stomatin PH1511 + H2O
?
Substrates: 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
Products: -
Products: -
?
p-stomatin PH1511p + H2O
?
Substrates: the N-terminal region of PH1510p is a serine protease and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
N-terminal region of open reading frame, PH1510 (residues 16236, designated as 1510-N) is a serine protease
UniProt
brenda
N-terminal region of open reading frame, PH1510 (residues 16236, designated as 1510-N) is a serine protease
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the local protein concentration of C-terminal region of enzyme PH1510 may be increased to promote self-assembly on the membrane surface by clustering the membrane-spanning regions (four membrane-spanning regions (residues 237-370) between protease domain 1510-N and OB-fold domain 1510-C) within the hydrophobic lipidbilayer
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme may be involved in the quality control of membrane proteins, e.g. stomatin, prohibitin, flotillin, and HflK/C domain proteins found in the lipid raft microdomains of various cellular membranes
additional information
additional information
the N-terminal region of PH1510p is a serine protease with a catalytic Ser-Lys dyad, Ser97 and Lys138
additional information
-
the N-terminal region of PH1510p is a serine protease with a catalytic Ser-Lys dyad, Ser97 and Lys138
additional information
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). The hexameric subcomplex I from archaeal proteasome consists of coiled-coil segments and oligonucleotide binding-fold domains, molecular modeling of hexameric oligonucleotide binding domains of enzyme 1510-C, domain structure, overview. Conserved residues at the domain surface may play key roles in maintaining protein-protein interactions of enzyme and substrate
additional information
-
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). The hexameric subcomplex I from archaeal proteasome consists of coiled-coil segments and oligonucleotide binding-fold domains, molecular modeling of hexameric oligonucleotide binding domains of enzyme 1510-C, domain structure, overview. Conserved residues at the domain surface may play key roles in maintaining protein-protein interactions of enzyme and substrate
additional information
C-terminal soluble enzyme domain 1510-C, residues 371-441 of PH1510, functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin
additional information
-
C-terminal soluble enzyme domain 1510-C, residues 371-441 of PH1510, functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). STOPP_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
441
0
48281
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
2 * 25000, dimer of the N-terminal fragment of PH1510 (1510-N, residues 16236), SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 25000, dimer of the N-terminal fragment of PH1510 (1510-N, residues 16236), SDS-PAGE
hexamer
molecular modeling of hexameric oligonucleotide binding domains of enzyme C-terminal region of enzyme PH1510 , inter-domain interactions and domain structure, overview
multimer
the structure of C-terminal soluble enzyme domain 1510-C, residues 371-441 of PH1510, has a compact five-stranded beta-barrel fold known as an oligosaccharide/oligonucleotide-binding fold (OB-fold). According to crystal packing, 1510-C can assemble into multimers based on a dimer as a basic unit. C-terminal soluble enzyme domain 1510-C also forms a large cylinder-like structure composed of 24 subunits or a large triangular prism-like structure composed of 12 subunits
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of 1510-N (N-terminal region of open reading frame, PH1510 (residues 16236)) in dimeric form
enzyme mutant K138A in complex with a peptide substrate, an enzyme dimer bound to one peptide, X-ray diffraction structure determination and analysis at 2.25 A resolution
hanging-drop vapor diffusion method, crystallization of the catalytically inactive mutants S97A and K138A of 1510-N in complex with three kinds of substrate peptides of p-stomatin (234NVIVLMLPME243, 232KSNVIVLML240 and 238LMLPMEMLK246), structural analysis
purified recombinant C-terminal soluble domain 1510-C of STOPP PH1510, sitting drop vapor diffusion method, mixing of 0.0005 ml of 5.7 mg/ml protein in 50 mM Tris-HCl, pH 7.5, and 50 mM NaCl with 0.0005 ml of reservoir solution containing 20% v/v Jeffamine M-600 and 0.1 M HEPES-NaOH, pH 7.5, 20°C, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement, for modelling the structure with PDB ID 2EXD is used method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
K138A
S97A
mutant enzyme shows 0.08% activity with casein compared with the activity of the wild-type enzyme
T62A
mutant enzyme shows 5.5% activity with casein compared with the activity of the wild-type enzyme
K138A
mutant enzyme shows 1.2% activity with casein compared with the activity of the wild-type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of the N-terminal fragment of PH1510 (1510-N, residues 16236) expressed in Escherichia coli
recombinant His-tagged full-length enzyme from Escherichia coli strain BL21-CodonPlus by nickel affinity and anion exchange chromatography, followed by dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene maps of the Pyrococcus horikoshii genome containing two sets of STOPP/stomatin gene pairs, i.e. PH1510 (long-STOPP)/PH1511 (p-stomatin) and PH0471 (short-STOPP)/PH0470 (p-stomatin). Recombinant expression of His-tagged full-length enzyme in Escherichia coli strain BL21-CodonPlus
the N-terminal region of PH1510 (1510-N, residues 16236) is expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yokoyama, H.; Matsui, I.
A novel thermostable membrane protease forming an operon with a stomatin homolog from the hyperthermophilic archaebacterium Pyrococcus horikoshii
J. Biol. Chem.
280
6588-6594
2005
Pyrococcus horikoshii (O59179), Pyrococcus horikoshii
brenda
Yokoyama, H.; Matsui, E.; Akiba, T.; Harata, K.; Matsui, I.
Molecular structure of a novel membrane protease specific for a stomatin homolog from the hyperthermophilic archaeon Pyrococcus horikoshii
J. Mol. Biol.
358
1152-1164
2006
Pyrococcus horikoshii (O59179), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O59179)
brenda
Yokoyama, H.; Kobayashi, D.; Takizawa, N.; Fujii, S.; Matsui, I.
Structural and biochemical analysis of a thermostable membrane-bound stomatin-specific protease
J. Synchrotron Radiat.
20
933-937
2013
Pyrococcus horikoshii (O59179), Pyrococcus horikoshii
brenda
Yokoyama, H.; Takizawa, N.; Kobayashi, D.; Matsui, I.; Fujii, S.
Crystal structure of a membrane stomatin-specific protease in complex with a substrate peptide
Biochemistry
51
3872-3880
2012
Pyrococcus horikoshii (O59179), Pyrococcus horikoshii
brenda
Yokoyama, H.; Matsui, E.; Hiramoto, K.; Forterre, P.; Matsui, I.
Clustering of OB-fold domains of the partner protease complexed with trimeric stomatin from Thermococcales
Biochimie
95
1494-1501
2013
Pyrococcus horikoshii (O59179), Pyrococcus horikoshii
brenda
Yokoyama, H.; Matsui, I.
Crystal structure of the stomatin operon partner protein from Pyrococcus horikoshii indicates the formation of a multimeric assembly
FEBS open bio
4
804-812
2014
Pyrococcus horikoshii (O59179), Pyrococcus horikoshii
brenda
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