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Information on EC 3.4.21.B56 - Pyrococcus horikoshii membrane protease PH1510 and Organism(s) Pyrococcus horikoshii and UniProt Accession O59179

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Pyrococcus horikoshii
UNIPROT: O59179
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Pyrococcus horikoshii
Synonyms
1510-n, ph1510, 1510-c, ph1510p, stopp ph1510, stomatin operon partner protein, stomatin/stopp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1510-N
membrane stomatin-specific protease
-
stomatin operon partner protein
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-casein + H2O
?
show the reaction diagram
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
-
-
?
beta-casein + H2O
?
show the reaction diagram
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
-
-
?
p-stomatin PH1511 + H2O
?
show the reaction diagram
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
-
-
?
p-stomatin PH1511p + H2O
?
show the reaction diagram
the N-terminal region of PH1510p is a serine protease and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p
-
-
?
stomatin-homolog PH1511 + H2O
?
show the reaction diagram
the N-terminal region of an open reading frame, PH1510 (residues 16–236, 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
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
p-stomatin PH1511 + H2O
?
show the reaction diagram
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
-
-
?
p-stomatin PH1511p + H2O
?
show the reaction diagram
the N-terminal region of PH1510p is a serine protease and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloroisocoumarin
1 mM, 49% inhibition
CaCl2
0.1 M, 11% activity
dodecyl-beta-D-maltoside
0.1%, 38% activity
EDTA
5 mM, 67% inhibition
iodoacetate
5 mM, 17% inhibition
MgCl2
0.1 M, 14% residual activity
MnCl2
0.1 M, 4% activity
NaCl
0.1 M, 90% loss of activity
pepstatin
0.005 mM, 21% inhibition
phenylmethylsulfonyl fluoride
5 mM, 21% inhibition
SDS
0.01%, 53% activity. 1% SDS, 1.2% activity
ZnCl2
0.1 M, 9% activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
2 * 25000, dimer of the N-terminal fragment of PH1510 (1510-N, residues 16–236), SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 25000, dimer of the N-terminal fragment of PH1510 (1510-N, residues 16–236), 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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of 1510-N (N-terminal region of open reading frame, PH1510 (residues 16–236)) 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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of the N-terminal fragment of PH1510 (1510-N, residues 16–236) 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
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 16–236) is expressed in Escherichia coli
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team