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 (LPD) (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of alpha-ketoacid dehydrogenase complexes)

 DLDH_CORGL              Reviewed;         469 AA.
Q8NTE1; Q6M7Z6; Q9Z466;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
20-DEC-2017, entry version 122.
RecName: Full=Dihydrolipoyl dehydrogenase;
Short=LPD;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
AltName: Full=E3 component of alpha-ketoacid dehydrogenase complexes;
Name=lpd; OrderedLocusNames=Cgl0366, cg0441;
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
LMG 3730 / NCIMB 10025).
Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
Corynebacterium.
NCBI_TaxID=196627;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-15, FUNCTION,
CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=11495999;
Schwinde J.W., Hertz P.F., Sahm H., Eikmanns B.J., Guyonvarch A.;
"Lipoamide dehydrogenase from Corynebacterium glutamicum: molecular
and physiological analysis of the lpd gene and characterization of the
enzyme.";
Microbiology 147:2223-2231(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
Ikeda M., Nakagawa S.;
"The Corynebacterium glutamicum genome: features and impacts on
biotechnological processes.";
Appl. Microbiol. Biotechnol. 62:99-109(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
Tauch A.;
"The complete Corynebacterium glutamicum ATCC 13032 genome sequence
and its impact on the production of L-aspartate-derived amino acids
and vitamins.";
J. Biotechnol. 104:5-25(2003).
[4]
IDENTIFICATION IN THE ODH/PDH COMPLEX.
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=16522631; DOI=10.1074/jbc.M512515200;
Niebisch A., Kabus A., Schultz C., Weil B., Bott M.;
"Corynebacterial protein kinase G controls 2-oxoglutarate
dehydrogenase activity via the phosphorylation status of the OdhI
protein.";
J. Biol. Chem. 281:12300-12307(2006).
-!- FUNCTION: Lipoamide dehydrogenase is an essential component of the
pyruvate dehydrogenase (PDH) and 2-oxoglutarate dehydrogenase
(ODH) complexes. Catalyzes the reoxidation of dihydrolipoyl groups
which are covalently attached to the lipoate acyltransferase
components (E2) of the complexes. Also catalyzes a reversible
NADH:NAD(+) transhydrogenation, and is able to transfer electrons
from NADH to various redox-active compounds and quinones. May be
involved in quinone redox cycling in C.glutamicum.
{ECO:0000269|PubMed:11495999}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH. {ECO:0000269|PubMed:11495999}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:11495999};
Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11495999};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.636 uM for lipoate {ECO:0000269|PubMed:11495999};
pH dependence:
Optimum pH is 7.0-7.5 for the reduction of lipoate by NADH.
{ECO:0000269|PubMed:11495999};
Temperature dependence:
Optimum temperature is 50 degrees Celsius for the reduction of
lipoate by NADH. {ECO:0000269|PubMed:11495999};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
-!- SUBUNIT: Homodimer (By similarity). Part of an unusual ODH/PDH
supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3)
together with OdhA (E1+E2). {ECO:0000250,
ECO:0000269|PubMed:16522631}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11495999}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
{ECO:0000250}.
-!- MISCELLANEOUS: Overexpression of LPD enhances sensitivity to
menadione, but has no effect on sensitivity to paraquat or
hydrogen peroxide.
-!- 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; Y16642; CAA76340.1; -; Genomic_DNA.
EMBL; BA000036; BAB97759.1; -; Genomic_DNA.
EMBL; BX927149; CAF19080.1; -; Genomic_DNA.
RefSeq; NP_599614.1; NC_003450.3.
RefSeq; WP_011013602.1; NC_006958.1.
ProteinModelPortal; Q8NTE1; -.
SMR; Q8NTE1; -.
STRING; 196627.cg0441; -.
EnsemblBacteria; BAB97759; BAB97759; BAB97759.
EnsemblBacteria; CAF19080; CAF19080; cg0441.
GeneID; 1021410; -.
KEGG; cgb:cg0441; -.
KEGG; cgl:NCgl0355; -.
PATRIC; fig|196627.13.peg.366; -.
eggNOG; ENOG4107QN2; Bacteria.
eggNOG; COG1249; LUCA.
HOGENOM; HOG000276708; -.
KO; K00382; -.
OMA; TMSEAVM; -.
BioCyc; CORYNE:G18NG-9923-MONOMER; -.
BRENDA; 1.8.1.4; 960.
UniPathway; UPA00223; UER00997.
Proteomes; UP000000582; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron transfer 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.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 3.
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;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase;
Redox-active center; Reference proteome; Tricarboxylic acid cycle.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11495999}.
CHAIN 2 469 Dihydrolipoyl dehydrogenase.
/FTId=PRO_0000420523.
NP_BIND 34 42 FAD. {ECO:0000250}.
NP_BIND 179 183 NAD. {ECO:0000250}.
NP_BIND 269 272 NAD. {ECO:0000250}.
ACT_SITE 448 448 Proton acceptor. {ECO:0000250}.
BINDING 51 51 FAD. {ECO:0000250}.
BINDING 114 114 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 202 202 NAD. {ECO:0000250}.
BINDING 312 312 FAD. {ECO:0000250}.
BINDING 320 320 FAD; via amide nitrogen. {ECO:0000250}.
DISULFID 42 47 Redox-active. {ECO:0000250}.
CONFLICT 382 382 F -> L (in Ref. 1; CAA76340).
{ECO:0000305}.
SEQUENCE 469 AA; 50652 MW; 7F8FFE6B510B8725 CRC64;
MTEHYDVVVL GAGPGGYVSA IRAAQLGKKV AVIEKQYWGG VCLNVGCIPS KSLIKNAEVA
HTFTHEKKTF GINGEVTFNY EDAHKRSRGV SDKIVGGVHY LMKKNKIIEI HGLGNFKDAK
TLEVTDGKDA GKTITFDDCI IATGSVVNTL RGVDFSENVV SFEEQILNPV APKKMVIVGA
GAIGMEFAYV LGNYGVDVTV IEFMDRVLPN EDAEVSKVIA KAYKKMGVKL LPGHATTAVR
DNGDFVEVDY QKKGSDKTET LTVDRVMVSV GFRPRVEGFG LENTGVKLTE RGAIEIDDYM
RTNVDGIYAI GDVTAKLQLA HVAEAQGIVA AETIAGAETQ TLGDYMMMPR ATFCNPQVSS
FGYTEEQAKE KWPDREIKVA SFPFSANGKA VGLAETDGFA KIVADAEFGE LLGAHLVGAN
ASELINELVL AQNWDLTTEE ISRSVHIHPT LSEAVKEAAH GISGHMINF


Related products :

Catalog number Product name Quantity
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
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
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
EIAAB28640 BCKADE2,BCKAD-E2,Bos taurus,Bovine,Branched-chain alpha-keto acid dehydrogenase complex component E2,DBT,Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase co
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
EIAAB28693 Bos taurus,Bovine,Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex,E3-binding protein,E3BP,PDHX,PDX1,proX,Pyruvate dehydrogenase protein X component
EIAAB28679 2-oxoglutarate dehydrogenase complex component E2,Bos taurus,Bovine,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransfera
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,
EIAAB11373 Canis familiaris,Canis lupus familiaris,Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,Dog
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
E1923b ELISA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Bos taurus,Bovine,OGDC-E1,OGDH 96T
U1923b CLIA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Bos taurus,Bovine,OGDC-E1,OGDH 96T
U1923b CLIA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Bos taurus,Bovine,OGDC-E1,OGDH 96T
E1923b ELISA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Bos taurus,Bovine,OGDC-E1,OGDH 96T
EIAAB28707 2-oxoglutarate dehydrogenase complex component E1-like,2-oxoglutarate dehydrogenase-like, mitochondrial,Alpha-ketoglutarate dehydrogenase-like,Homo sapiens,Human,KIAA1290,OGDC-E1-like,OGDHL
E1923m ELISA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Kiaa4192,Mouse,Mus musculus,OGDC-E1,Ogdh 96T
U1923r CLIA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,OGDC-E1,Ogdh,Ogdhl,Rat,Rattus norvegicus 96T
U1923h CLIA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Homo sapiens,Human,OGDC-E1,OGDH 96T
U1923m CLIA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Kiaa4192,Mouse,Mus musculus,OGDC-E1,Ogdh 96T
E1923r ELISA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,OGDC-E1,Ogdh,Ogdhl,Rat,Rattus norvegicus 96T
E1923m ELISA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Kiaa4192,Mouse,Mus musculus,OGDC-E1,Ogdh 96T
U1923m CLIA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Kiaa4192,Mouse,Mus musculus,OGDC-E1,Ogdh 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