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

Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 1 (EC 5.1.3.2) (EC 5.1.3.5) (UDP-D-xylose 4-epimerase) (UDP-L-arabinose 4-epimerase) (UDP-galactose 4-epimerase 1) (UDP-glucose 4-epimerase 1) (PsUGE1)

 UGE1_PEA                Reviewed;         350 AA.
B0M3E8;
01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 2.
25-OCT-2017, entry version 41.
RecName: Full=Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 1;
EC=5.1.3.2;
EC=5.1.3.5;
AltName: Full=UDP-D-xylose 4-epimerase;
AltName: Full=UDP-L-arabinose 4-epimerase;
AltName: Full=UDP-galactose 4-epimerase 1;
AltName: Full=UDP-glucose 4-epimerase 1;
Short=PsUGE1;
Name=UGE1;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-30, FUNCTION,
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=19754426; DOI=10.1042/BJ20091025;
Kotake T., Takata R., Verma R., Takaba M., Yamaguchi D., Orita T.,
Kaneko S., Matsuoka K., Koyama T., Reiter W.D., Tsumuraya Y.;
"Bifunctional cytosolic UDP-glucose 4-epimerases catalyse the
interconversion between UDP-D-xylose and UDP-L-arabinose in plants.";
Biochem. J. 424:169-177(2009).
-!- FUNCTION: Catalyzes the interconversion between UDP-glucose and
UDP-galactose and the interconversion between UDP-arabinose and
UDP-xylose. {ECO:0000269|PubMed:19754426}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-alpha-D-galactose.
-!- CATALYTIC ACTIVITY: UDP-L-arabinose = UDP-D-xylose.
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Inhibited by Hg(2+).
{ECO:0000269|PubMed:19754426}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.29 mM for for UDP-galactose {ECO:0000269|PubMed:19754426};
KM=0.31 mM for for UDP-glucose {ECO:0000269|PubMed:19754426};
KM=0.15 mM for for UDP-xylose {ECO:0000269|PubMed:19754426};
KM=0.16 mM for for UDP-arabinose {ECO:0000269|PubMed:19754426};
pH dependence:
Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:19754426};
Temperature dependence:
Optimum temperature is 30 degrees Celsius.
{ECO:0000269|PubMed:19754426};
-!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-L-arabinose
biosynthesis; UDP-L-arabinose from UDP-alpha-D-xylose: step 1/1.
-!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide
biosynthesis.
-!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB381885; BAG09236.2; -; mRNA.
ProteinModelPortal; B0M3E8; -.
SMR; B0M3E8; -.
BRENDA; 5.1.3.2; 4872.
BRENDA; 5.1.3.5; 4872.
UniPathway; UPA00214; -.
UniPathway; UPA00797; UER00772.
UniPathway; UPA00963; -.
GO; GO:0050373; F:UDP-arabinose 4-epimerase activity; IDA:UniProtKB.
GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0033358; P:UDP-L-arabinose biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd05247; UDP_G4E_1_SDR_e; 1.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR005886; UDP_G4E.
Pfam; PF16363; GDP_Man_Dehyd; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01179; galE; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Cell wall biogenesis/degradation;
Direct protein sequencing; Galactose metabolism; Isomerase; NAD.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:19754426}.
CHAIN 2 350 Bifunctional UDP-glucose 4-epimerase and
UDP-xylose 4-epimerase 1.
/FTId=PRO_0000422187.
NP_BIND 7 38 NAD. {ECO:0000250}.
ACT_SITE 157 157 Proton acceptor. {ECO:0000250}.
BINDING 133 133 Substrate. {ECO:0000250}.
SEQUENCE 350 AA; 38960 MW; FE583CD7CEB39D62 CRC64;
MVASSQKILV TGGAGFIGTH TVVQLLNNGF NVSIIDNFDN SVMEAVERVR EVVGSNLSQN
LEFTLGDLRN KDDLEKLFSK SKFDAVIHFA GLKAVGESVE NPRRYFDNNL VGTINLYEVM
AKHNCKKMVF SSSATVYGQP EKIPCVEDFK LQAMNPYGRT KLFLEEIARD IQKAEPEWRI
VLLRYFNPVG AHESGKLGED PRGIPNNLMP YIQQVAVGRL PELNVYGHDY PTRDGSAIRD
YIHVMDLADG HIAALRKLFT SENIGCTAYN LGTGRGSSVL EMVAAFEKAS GKKIALKLCP
RRPGDATEVY ASTAKAEKEL GWKAKYGVEE MCRDQWNWAK NNPWGYSGKP


Related products :

Catalog number Product name Quantity
EIAAB11961 Bos taurus,Bovine,Chondroitin-glucuronate 5-epimerase,Dermatan-sulfate epimerase,DS epimerase,DSE
EIAAB34262 AGE,GlcNAc 2-epimerase,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,Pig,RENBP,Renin-binding protein,RnBP,Sus scrofa
EIAAB34257 AGE,Bos taurus,Bovine,GlcNAc 2-epimerase,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,RENBP,Renin-binding protein,RnBP
EIAAB34259 AGE,GlcNAc 2-epimerase,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,Rat,Rattus norvegicus,Renbp,Renin-binding protein,RnBP
EIAAB34260 AGE,GlcNAc 2-epimerase,Mouse,Mus musculus,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,Renbp,Renin-binding protein,RnBP
EIAAB34261 AGE,GlcNAc 2-epimerase,Homo sapiens,Human,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,RENBP,Renin-binding protein,RnBP
EIAAB11962 Chondroitin-glucuronate 5-epimerase,Dermatan-sulfate epimerase,DS epimerase,Dse,Mouse,Mus musculus,Sart2,SART-2,Squamous cell carcinoma antigen recognized by T-cells 2
EIAAB11963 Chondroitin-glucuronate 5-epimerase,Dermatan-sulfate epimerase,DS epimerase,DSE,Homo sapiens,Human,SART2,SART-2,Squamous cell carcinoma antigen recognized by T-cells 2
EIAAB34258 AGE,Canis familiaris,Canis lupus familiaris,Dog,GlcNAc 2-epimerase,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,RENBP,Renin-binding protein,RnBP
29-593 HSD17B6 has both oxidoreductase and epimerase activities and is involved in androgen catabolism. The oxidoreductase activity can convert 3 alpha-adiol to dihydrotestosterone, while the epimerase activ 0.1 mg
EIAAB35839 Homo sapiens,Human,HUSSY-17,Ribulose-5-phosphate-3-epimerase,Ribulose-phosphate 3-epimerase,RPE
EIAAB35838 Mouse,Mus musculus,Ribulose-5-phosphate-epimerase,Ribulose-phosphate 3-epimerase,Rpe
C263 UDP-Glucose 4-Epimerase GALE 500
C263 UDP-Glucose 4-Epimerase GALE lmg
E13897r Rat ELISA Kit FOR UDP-glucose 4-epimerase 96T
26-862 GALE is an UDP-galactose-4-epimerase which catalyzes two distinct but analogous reactions the epimerization of UDP-glucose to UDP-galactose, and the epimerization of UDP-N-acetylglucosamine to UDP-N- 0.05 mg
CG72 Human UDP-Glucose 4-Epimerase GALE 50
I0537 UDP-glucose 4-epimerase (GALE), Rat, ELISA Kit 96T
CSB-EL009197RA Rat UDP-glucose 4-epimerase(GALE) ELISA kit 96T
CG76 Human UDP-Glucose 4-Epimerase GALE l0
CSB-EL009197HU Human UDP-glucose 4-epimerase(GALE) ELISA kit 96T
CSB-EL009197RA Rat UDP-glucose 4-epimerase(GALE) ELISA kit SpeciesRat 96T
I0536 UDP-glucose 4-epimerase (GALE), Mouse, ELISA Kit 96T
CSB-EL009197MO Mouse UDP-glucose 4-epimerase(GALE) ELISA kit 96T
I0535 UDP-glucose 4-epimerase (GALE), Human, ELISA Kit 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