Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Deglycase PfpI (EC 3.5.1.124) (Intracellular protease I) (EC 3.4.22.-)

 DEGLY_PYRFU             Reviewed;         166 AA.
Q51732;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 105.
RecName: Full=Deglycase PfpI {ECO:0000303|PubMed:27530919};
EC=3.5.1.124 {ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919};
AltName: Full=Intracellular protease I {ECO:0000303|PubMed:8626329};
EC=3.4.22.- {ECO:0000269|PubMed:16535492};
Name=pfpI {ECO:0000303|PubMed:8626329}; OrderedLocusNames=PF1719;
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=186497;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-28; 128-157
AND 159-166, FUNCTION AS A PROTEASE, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, AND SUBUNIT.
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=8626329; DOI=10.1128/jb.178.9.2605-2612.1996;
Halio S.B., Blumentals I.I., Short S.A., Merrill B.M., Kelly R.M.;
"Sequence, expression in Escherichia coli, and analysis of the gene
encoding a novel intracellular protease (PfpI) from the
hyperthermophilic archaeon Pyrococcus furiosus.";
J. Bacteriol. 178:2605-2612(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=10430560;
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
DiRuggiero J., Robb F.T.;
"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and
P. horikoshii inferred from complete genomic sequences.";
Genetics 152:1299-1305(1999).
[3]
FUNCTION AS A PROTEASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBUNIT.
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=16535492;
Halio S.B., Bauer M.W., Mukund S., Adams M., Kelly R.M.;
"Purification and characterization of two functional forms of
intracellular protease PfpI from the hyperthermophilic archaeon
Pyrococcus furiosus.";
Appl. Environ. Microbiol. 63:289-295(1997).
[4]
FUNCTION AS A DEGLYCASE, AND BIOTECHNOLOGY.
PubMed=27530919; DOI=10.1016/j.bbrc.2016.08.077;
Richarme G., Marguet E., Forterre P., Ishino S., Ishino Y.;
"DJ-1 family Maillard deglycases prevent acrylamide formation.";
Biochem. Biophys. Res. Commun. 478:1111-1116(2016).
-!- FUNCTION: Deglycase that catalyzes the deglycation of the Maillard
adducts formed between amino groups of proteins and reactive
carbonyl groups of glyoxals (Probable). Thus, functions as a
protein deglycase that repairs methylglyoxal- and glyoxal-glycated
proteins, and releases repaired proteins and lactate or glycolate,
respectively (PubMed:27530919). Deglycates cysteine, arginine and
lysine residues in proteins, and thus reactivates these proteins
by reversing glycation by glyoxals (By similarity). Thus, was
shown to afford full protection against glycation of thioredoxin
by glyoxal (PubMed:27530919). Acts on early glycation
intermediates (hemithioacetals and aminocarbinols), preventing the
formation of advanced glycation endproducts (AGE) that cause
irreversible damage (By similarity). Prevents acrylamide formation
in asparagine/glyoxal and asparagine/sugar mixtures, likely by
degrading asparagine/glyoxal Maillard adducts formed at high
temperatures (PubMed:27530919). Also displays proteolytic activity
(PubMed:8626329, PubMed:16535492). Cleaves at the carboxyl side of
both basic and hydrophobic residues in the P1 position, indicating
trypsin- and chymotrypsin-like specificities (PubMed:16535492).
{ECO:0000250|UniProtKB:P45470, ECO:0000269|PubMed:16535492,
ECO:0000269|PubMed:27530919, ECO:0000269|PubMed:8626329}.
-!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-
L-arginine + H(2)O = a [protein]-L-arginine + (R)-lactate.
{ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919}.
-!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-
lysine + H(2)O = a [protein]-L-lysine + (R)-lactate.
{ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919}.
-!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxopropyl)-[protein]-L-
cysteine + H(2)O = a [protein]-L-cysteine + (R)-lactate.
{ECO:0000250|UniProtKB:P45470, ECO:0000305|PubMed:27530919}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.3 for proteolytic activity with AAF-MCA as
substrate. {ECO:0000269|PubMed:16535492};
Temperature dependence:
Optimum temperature is 84-97 degrees Celsius for proteolytic
activity (PubMed:8626329, PubMed:16535492). Thermostable.
Displays a half-life of 19 minutes at 95 degrees Celsius
(PubMed:8626329). {ECO:0000269|PubMed:16535492,
ECO:0000269|PubMed:8626329};
-!- SUBUNIT: Homooligomer (PubMed:8626329). Exists in two functional
species: the predominant form is a homohexamer that comprises
about 90% of the total activity, and the minor form is trimeric
(PubMed:16535492). {ECO:0000269|PubMed:16535492,
ECO:0000269|PubMed:8626329}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8626329}.
-!- BIOTECHNOLOGY: Being able to prevent acrylamide formation at 100
degrees Celsius, this enzyme could constitute a viable and unique
enzymatic method to reduce acrylamide formation in food, whose
presence is a worldwide concern because it is carcinogenic,
reprotoxic and neurotoxic. The use of deglycases is not likely to
affect the quality parameters of foods, in contrast with methods
which lead to depletion of the components (asparagine and sugars)
responsible for acrylamide formation. Moreover, deglycases can be
used directly during the thermal process, which avoids a time
consuming pre-incubation step. Consequently, many foods whose
heating processes occur at around 100 degrees Celsius, such as
baby foods, evaporated milk, dry soups and prune juices could be
clients of the deglycase method. {ECO:0000305|PubMed:27530919}.
-!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U57642; AAB04694.1; -; Genomic_DNA.
EMBL; AE009950; AAL81843.1; -; Genomic_DNA.
PIR; JC6003; JC6003.
RefSeq; WP_011012865.1; NC_003413.1.
ProteinModelPortal; Q51732; -.
SMR; Q51732; -.
STRING; 186497.PF1719; -.
MEROPS; C56.001; -.
PRIDE; Q51732; -.
EnsemblBacteria; AAL81843; AAL81843; PF1719.
GeneID; 1469596; -.
KEGG; pfu:PF1719; -.
PATRIC; fig|186497.12.peg.1787; -.
eggNOG; arCOG00769; Archaea.
eggNOG; COG0693; LUCA.
HOGENOM; HOG000063195; -.
KO; K05520; -.
OMA; MVGHTVH; -.
OrthoDB; POG093Z0CI8; -.
BRENDA; 3.4.22.B20; 5243.
Proteomes; UP000001013; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
Gene3D; 3.40.50.880; -; 1.
InterPro; IPR006286; C56_PfpI.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR002818; DJ-1/PfpI.
Pfam; PF01965; DJ-1_PfpI; 1.
SUPFAM; SSF52317; SSF52317; 1.
TIGRFAMs; TIGR01382; PfpI; 1.
PROSITE; PS51276; PEPTIDASE_C56_PFPI; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase;
Protease; Reference proteome.
CHAIN 1 166 Deglycase PfpI.
/FTId=PRO_0000157826.
DOMAIN 1 166 PfpI endopeptidase. {ECO:0000255|PROSITE-
ProRule:PRU00608}.
ACT_SITE 100 100 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00608}.
ACT_SITE 101 101 {ECO:0000255|PROSITE-ProRule:PRU00608}.
SEQUENCE 166 AA; 18791 MW; B4AA6FFB83FBE52F CRC64;
MKILFLSANE FEDVELIYPY HRLKEEGHEV YIASFEKGVI TGKHGYSVKV DLTFDEVNPD
EFDALVLPGG RAPERVRLNE KAVEIARKMF TEGKPVATIC HGPQILISAG VLKGRKGTSY
IGIRDDMINA GVEWIDREVV VDGNWVSSRH PGDLYAWMRE FVKLLK


Related products :

Catalog number Product name Quantity
26-943 PLDN may play a role in intracellular vesicle trafficking. It interacts with Syntaxin 13 which mediates intracellular membrane fusion.The protein encoded by this gene may play a role in intracellular 0.05 mg
30-111 CSTB is a stefin that functions as an intracellular thiol protease inhibitor. The protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. The pro 0.05 mg
30-112 CSTB is a stefin that functions as an intracellular thiol protease inhibitor. The protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. The pro 0.05 mg
orb90001 GST_HRV Protease Protease Recombinant is fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes subset of sequences whic 100 IU
orb90006 Tobacco Etch Virus Protease protein Recombinant TEV Protease (rTEV) is site-specific protease purified from E.coli The protease can be used for the removal of affinity tags from fusion proteins. The s 300 IU
orb82817 PreScission Protease enzyme PreScission Protease is a fusion protein of Glutathione S-Transferase (GST) and Human Rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of 1000 U
orb82840 Tobacco Etch Virus Protease enzyme Recombinant TEV Protease (rTEV) is a site-specific protease purified from E. coli by the affinity tag, GST tag. The protease can be used for the removal of affinity 1000 IU
25-910 Sodium-hydrogen exchangers (NHEs), such as SLC9A8, are integral transmembrane proteins that exchange extracellular Na+ for intracellular H+. NHEs have multiple functions, including intracellular pH ho 0.05 mg
U2015h CLIA Apoptotic cysteine protease,Apoptotic protease Mch-5,CAP4,CASP8,CASP-8,Caspase-8,FADD-homologous ICE_ced-3-like protease,FADD-like ICE,FLICE,Homo sapiens,Human,ICE-like apoptotic protease 5,MACH, 96T
E2015h ELISA Apoptotic cysteine protease,Apoptotic protease Mch-5,CAP4,CASP8,CASP-8,Caspase-8,FADD-homologous ICE_ced-3-like protease,FADD-like ICE,FLICE,Homo sapiens,Human,ICE-like apoptotic protease 5,MACH 96T
U2015h CLIA kit Apoptotic cysteine protease,Apoptotic protease Mch-5,CAP4,CASP8,CASP-8,Caspase-8,FADD-homologous ICE_ced-3-like protease,FADD-like ICE,FLICE,Homo sapiens,Human,ICE-like apoptotic protease 5, 96T
E2015h ELISA kit Apoptotic cysteine protease,Apoptotic protease Mch-5,CAP4,CASP8,CASP-8,Caspase-8,FADD-homologous ICE_ced-3-like protease,FADD-like ICE,FLICE,Homo sapiens,Human,ICE-like apoptotic protease 5 96T
EIAAB37886 DEN1,Deneddylase-1,FKSG8,Homo sapiens,Human,NEDD8-specific protease 1,NEDP1,Protease, cysteine 2,PRSC2,SENP8,Sentrin_SUMO-specific protease SENP8,Sentrin-specific protease 8
E0691h ELISA kit Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T
E0691h ELISA Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T
U0691h CLIA Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T
EIAAB42592 Adrenal secretory serine protease,Airway trypsin-like protease,AsP,AT,Mat,Mouse,Mus musculus,Tmprss11d,Transmembrane protease serine 11D
EIAAB42593 Adrenal secretory serine protease,Airway trypsin-like protease,AsP,AT,Rat,Rat,Rattus norvegicus,Tmprss11d,Transmembrane protease serine 11D
EIAAB43231 CAPH2,Channel-activating protease 2,Homo sapiens,Human,Membrane-type serine protease 2,MT-SP2,TMPRSS3,TMPRSS4,Transmembrane protease serine 4,UNQ776_PRO1570
30-350 ST14 is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-pho 0.05 mg
EIAAB44303 Cancer_testis antigen 20,CT20,Homo sapiens,Human,Probable threonine protease PRSS50,PRSS50,Serine protease 50,Testis-specific protease-like protein 50,TSP50
EIAAB32605 Disp,Distal intestinal serine protease,Prss30,Rat,Rattus norvegicus,Serine protease 30,Tmprss8,Tmsp1,TMSP-1,Tmsp-1,Transmembrane serine protease 1,Transmembrane serine protease 8
U0627h CLIA APAF-3,Apoptotic protease Mch-6,Apoptotic protease-activating factor 3,CASP9,CASP-9,Caspase-9,Homo sapiens,Human,ICE-LAP6,ICE-like apoptotic protease 6,MCH6 96T
E0627h ELISA kit APAF-3,Apoptotic protease Mch-6,Apoptotic protease-activating factor 3,CASP9,CASP-9,Caspase-9,Homo sapiens,Human,ICE-LAP6,ICE-like apoptotic protease 6,MCH6 96T
E0627h ELISA APAF-3,Apoptotic protease Mch-6,Apoptotic protease-activating factor 3,CASP9,CASP-9,Caspase-9,Homo sapiens,Human,ICE-LAP6,ICE-like apoptotic protease 6,MCH6 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur