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

Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of pyruvate complex)

 DLDH_AZOVI              Reviewed;         477 AA.
P18925;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
22-NOV-2017, entry version 127.
RecName: Full=Dihydrolipoyl dehydrogenase;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
AltName: Full=E3 component of pyruvate complex;
Azotobacter vinelandii.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Azotobacter.
NCBI_TaxID=354;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2832161; DOI=10.1111/j.1432-1033.1988.tb13887.x;
Westphal A.H., de Kok A.;
"Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular
cloning, organization and sequence analysis of the gene.";
Eur. J. Biochem. 172:299-305(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21, AND DISULFIDE BOND.
PubMed=2404760; DOI=10.1111/j.1432-1033.1990.tb15300.x;
Westphal A.H., de Kok A.;
"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii.
2. Molecular cloning and sequence analysis of the gene encoding the
succinyltransferase component.";
Eur. J. Biochem. 187:235-239(1990).
[3]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH FAD.
PubMed=1880807; DOI=10.1016/0022-2836(91)90367-F;
Mattevi A., Schierbeek A.J., Hol W.G.J.;
"Refined crystal structure of lipoamide dehydrogenase from Azotobacter
vinelandii at 2.2-A resolution. A comparison with the structure of
glutathione reductase.";
J. Mol. Biol. 220:975-994(1991).
-!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
conversion of pyruvate to acetyl-CoA and CO(2). It contains
multiple copies of three enzymatic components: pyruvate
dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
lipoamide dehydrogenase (E3).
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1880807}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M37307; AAA22139.1; -; Genomic_DNA.
EMBL; X52432; CAA36679.1; -; Genomic_DNA.
PIR; S00360; DEAVHL.
RefSeq; WP_012701528.1; NZ_FPKM01000019.1.
PDB; 3LAD; X-ray; 2.20 A; A/B=2-477.
PDBsum; 3LAD; -.
ProteinModelPortal; P18925; -.
SMR; P18925; -.
DrugBank; DB03147; Flavin adenine dinucleotide.
eggNOG; ENOG4107QN2; Bacteria.
eggNOG; COG1249; LUCA.
SABIO-RK; P18925; -.
EvolutionaryTrace; P18925; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; Disulfide bond; FAD; Flavoprotein;
Glycolysis; NAD; Oxidoreductase; Redox-active center.
CHAIN 1 477 Dihydrolipoyl dehydrogenase.
/FTId=PRO_0000068014.
NP_BIND 34 49 FAD. {ECO:0000269|PubMed:1880807}.
NP_BIND 188 192 NAD. {ECO:0000250}.
NP_BIND 276 279 NAD. {ECO:0000250}.
ACT_SITE 451 451 Proton acceptor.
BINDING 58 58 FAD. {ECO:0000269|PubMed:1880807}.
BINDING 122 122 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 211 211 NAD. {ECO:0000250}.
BINDING 245 245 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 319 319 FAD. {ECO:0000269|PubMed:1880807}.
BINDING 327 327 FAD; via amide nitrogen.
{ECO:0000269|PubMed:1880807}.
DISULFID 49 54 Redox-active.
{ECO:0000269|PubMed:1880807,
ECO:0000269|PubMed:2404760}.
STRAND 6 10 {ECO:0000244|PDB:3LAD}.
HELIX 14 26 {ECO:0000244|PDB:3LAD}.
STRAND 30 34 {ECO:0000244|PDB:3LAD}.
STRAND 41 43 {ECO:0000244|PDB:3LAD}.
HELIX 47 52 {ECO:0000244|PDB:3LAD}.
HELIX 54 71 {ECO:0000244|PDB:3LAD}.
HELIX 75 77 {ECO:0000244|PDB:3LAD}.
HELIX 88 113 {ECO:0000244|PDB:3LAD}.
STRAND 116 124 {ECO:0000244|PDB:3LAD}.
STRAND 130 133 {ECO:0000244|PDB:3LAD}.
STRAND 139 142 {ECO:0000244|PDB:3LAD}.
STRAND 147 149 {ECO:0000244|PDB:3LAD}.
STRAND 153 155 {ECO:0000244|PDB:3LAD}.
STRAND 165 170 {ECO:0000244|PDB:3LAD}.
HELIX 171 174 {ECO:0000244|PDB:3LAD}.
STRAND 182 187 {ECO:0000244|PDB:3LAD}.
HELIX 191 202 {ECO:0000244|PDB:3LAD}.
STRAND 206 217 {ECO:0000244|PDB:3LAD}.
HELIX 222 234 {ECO:0000244|PDB:3LAD}.
STRAND 237 241 {ECO:0000244|PDB:3LAD}.
STRAND 244 250 {ECO:0000244|PDB:3LAD}.
STRAND 255 275 {ECO:0000244|PDB:3LAD}.
STRAND 279 281 {ECO:0000244|PDB:3LAD}.
STRAND 314 316 {ECO:0000244|PDB:3LAD}.
HELIX 318 320 {ECO:0000244|PDB:3LAD}.
STRAND 321 323 {ECO:0000244|PDB:3LAD}.
HELIX 327 343 {ECO:0000244|PDB:3LAD}.
STRAND 355 357 {ECO:0000244|PDB:3LAD}.
STRAND 359 367 {ECO:0000244|PDB:3LAD}.
HELIX 370 375 {ECO:0000244|PDB:3LAD}.
STRAND 380 386 {ECO:0000244|PDB:3LAD}.
HELIX 387 389 {ECO:0000244|PDB:3LAD}.
HELIX 391 396 {ECO:0000244|PDB:3LAD}.
STRAND 402 408 {ECO:0000244|PDB:3LAD}.
TURN 409 411 {ECO:0000244|PDB:3LAD}.
STRAND 413 421 {ECO:0000244|PDB:3LAD}.
HELIX 424 436 {ECO:0000244|PDB:3LAD}.
HELIX 441 445 {ECO:0000244|PDB:3LAD}.
HELIX 455 465 {ECO:0000244|PDB:3LAD}.
SEQUENCE 477 AA; 49567 MW; 4219A8EA4DAFCAD0 CRC64;
MSQKFDVIVI GAGPGGYVAA IKSAQLGLKT ALIEKYKGKE GKTALGGTCL NVGCIPSKAL
LDSSYKFHEA HESFKLHGIS TGEVAIDVPT MIARKDQIVR NLTGGVASLI KANGVTLFEG
HGKLLAGKKV EVTAADGSSQ VLDTENVILA SGSKPVEIPP APVDQDVIVD STGALDFQNV
PGKLGVIGAG VIGLELGSVW ARLGAEVTVL EAMDKFLPAV DEQVAKEAQK ILTKQGLKIL
LGARVTGTEV KNKQVTVKFV DAEGEKSQAF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF
IYVDDYCATS VPGVYAIGDV VRGAMLAHKA SEEGVVVAER IAGHKAQMNY DLIPAVIYTH
PEIAGVGKTE QALKAEGVAI NVGVFPFAAS GRAMAANDTA GFVKVIADAK TDRVLGVHVI
GPSAAELVQQ GAIAMEFGTS AEDLGMMVFA HPALSEALHE AALAVSGHAI HVANRKK


Related products :

Catalog number Product name Quantity
EIAAB28692 Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex,Lipoyl-containing pyruvate dehydrogenase complex component X,Mouse,Mus musculus,Pdhx,Pyruvate dehydrogenase protein X c
15-288-22844 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex. mitochondrial - EC 2.3.1.12; Pyruvate dehydrogenase complex E2 subunit; PDCE2; E2; Dihydrolipoamide S-acetylt 0.05 mg
15-288-22844 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex. mitochondrial - EC 2.3.1.12; Pyruvate dehydrogenase complex E2 subunit; PDCE2; E2; Dihydrolipoamide S-acetylt 0.1 mg
18-003-43720 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex. mitochondrial - EC 2.3.1.12; Pyruvate dehydrogenase complex E2 subunit; PDCE2; E2; Dihydrolipoamide S-acetylt 0.1 mg Protein A
EIAAB28682 Bos taurus,Bovine,Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex,Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex,DLAT,Pyruvate
EIAAB28681 Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex,Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial,Dlat,Mouse,Mus m
EIAAB28691 Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex,E3-binding protein,E3BP,Homo sapiens,Human,Lipoyl-containing pyruvate dehydrogenase complex component X,PDHX,PDX1,proX,
EIAAB28693 Bos taurus,Bovine,Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex,E3-binding protein,E3BP,PDHX,PDX1,proX,Pyruvate dehydrogenase protein X component
27-169 DLD is the L protein of the mitochondrial glycine cleavage system. The L protein, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvate dehydrogenase complex, the alpha-ketogl 0.05 mg
18-783-77883 RABBIT ANTI PORCINE LIPOAMIDE DEHYDROGENASE - EC 1.8.1.4; Dihydrolipoamide dehydrogenase; Pyruvate dehydrogenase complex E3 subunit; PDC-E3; E3; Glycine cleavage system L protein Polyclonal 1 ml
GWB-C1EDDF Anti- DLAT (dihydrolipoamide S-acetyltransferase (E2 component of pyruvate dehydrogenase complex)) Antibody
EIAAB28679 2-oxoglutarate dehydrogenase complex component E2,Bos taurus,Bovine,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransfera
EIAAB28680 70 kDa mitochondrial autoantigen of primary biliary cirrhosis,Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex,Dihydrolipoyllysine-residue acetyltransferase component of
EIAAB28683 70 kDa mitochondrial autoantigen of primary biliary cirrhosis,Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex,Dihydrolipoyllysine-residue acetyltransferase component of
EIAAB28675 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB28676 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB28677 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB28678 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB11371 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,Dld,Mouse,Mus musculus
EIAAB11375 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,Dld,Rat,Rattus norvegicus
EIAAB11374 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,LAD,Pig,Sus scrofa
EIAAB11372 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,GCSL,Glycine cleavage system L protein,Homo sapiens,Human,LAD,PHE3
EIAAB28639 BCATE2,BCKADE2,BCKAD-E2,Branched-chain alpha-keto acid dehydrogenase complex component E2,DBT,Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex,Dihyd
EIAAB28638 BCKADE2,BCKAD-E2,Branched-chain alpha-keto acid dehydrogenase complex component E2,Dbt,Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex,Dihydrolipoa
26-287 The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components pyruvate dehydrogenase (E1), dihydroli 0.05 mg


 

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