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, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase)

 DLDH_CRIGR              Reviewed;         509 AA.
Q8CIZ7;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
10-MAY-2017, entry version 82.
RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
EC=1.8.1.4 {ECO:0000250|UniProtKB:P09622};
AltName: Full=Dihydrolipoamide dehydrogenase;
Flags: Precursor;
Name=DLD;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Keightley J.A., Shang L., Kinter M.;
"2D gel analysis of the proteomic adaptation of a mammalian cell line
to oxidative stress reveals changes in the expression of metabolically
relevant enzymes.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
cleavage system as well as an E3 component of the alpha-ketoacid
dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and
branched-chain amino acid-dehydrogenase complex). In monomeric
form has additional moonlighting function as serine protease.
Involved in the hyperactivation of spermatazoa during capacitation
and in the spermatazoal acrosome reaction.
{ECO:0000250|UniProtKB:P09622, ECO:0000250|UniProtKB:Q811C4}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
{ECO:0000250|UniProtKB:P09622}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:P09622};
Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09622};
-!- SUBUNIT: Homodimer. Part of the multimeric pyruvate dehydrogenase
complex that contains multiple copies of pyruvate dehydrogenase
(subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase
(DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits
are bound to an inner core composed of about 48 DLAT and 12 PDHX
molecules (by non covalent bonds). Interacts with PDHX.
{ECO:0000250|UniProtKB:P09622}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000250|UniProtKB:P09622}. Cytoplasmic vesicle, secretory
vesicle, acrosome {ECO:0000250|UniProtKB:Q811C4}. Cell projection,
cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}.
-!- PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}.
-!- 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; AF539836; AAN15202.1; -; mRNA.
RefSeq; NP_001233626.1; NM_001246697.1.
ProteinModelPortal; Q8CIZ7; -.
SMR; Q8CIZ7; -.
PRIDE; Q8CIZ7; -.
GeneID; 100689437; -.
KEGG; cge:100689437; -.
CTD; 1738; -.
HOVERGEN; HBG002290; -.
KO; K00382; -.
GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
InterPro; IPR006258; Lipoamide_DH.
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.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
2: Evidence at transcript level;
Acetylation; Cell projection; Cilium; Cytoplasmic vesicle;
Disulfide bond; FAD; Flagellum; Flavoprotein; Mitochondrion; NAD;
Oxidoreductase; Phosphoprotein; Redox-active center; Transit peptide.
TRANSIT 1 35 Mitochondrion. {ECO:0000250}.
CHAIN 36 509 Dihydrolipoyl dehydrogenase,
mitochondrial.
/FTId=PRO_0000260226.
NP_BIND 71 80 FAD. {ECO:0000250}.
NP_BIND 183 185 FAD. {ECO:0000250}.
NP_BIND 220 227 NAD. {ECO:0000250}.
NP_BIND 361 364 FAD. {ECO:0000250}.
ACT_SITE 487 487 Proton acceptor. {ECO:0000250}.
BINDING 89 89 FAD. {ECO:0000250}.
BINDING 154 154 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 243 243 NAD. {ECO:0000250}.
BINDING 278 278 NAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 314 314 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 355 355 FAD. {ECO:0000250}.
SITE 448 448 Important for interaction with PDHX and
activity of pyruvate dehydrogenase
complex. {ECO:0000250|UniProtKB:P09622}.
SITE 473 473 Important for interaction with PDHX and
activity of pyruvate dehydrogenase
complex. {ECO:0000250|UniProtKB:P09622}.
MOD_RES 66 66 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 66 66 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 122 122 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 122 122 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 132 132 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 132 132 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 143 143 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P09622}.
MOD_RES 143 143 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 159 159 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 166 166 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 273 273 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 277 277 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6R2}.
MOD_RES 346 346 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 410 410 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P09622}.
MOD_RES 410 410 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 417 417 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09622}.
MOD_RES 420 420 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 430 430 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000250|UniProtKB:P09622}.
MOD_RES 505 505 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 505 505 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
DISULFID 80 85 Redox-active. {ECO:0000250}.
SEQUENCE 509 AA; 54131 MW; FADBCF01E42576AB CRC64;
MQSWSRVYCS LAKRGHFNRI SHGLQGVSSV PLRTYADQPI DADVTVIGSG PGGYVAAIKA
AQLGFKTVCI EKNDTLGGTC LNVGCIPSKA LLNNSHYYHL AHGRDFASRG IELSEVRLNL
EKMMEQKSSA VKALIGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS SQVIGTKNIL
IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT
AVEFLGHVGG IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKRSDGKID VSVEAASGGK
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK
FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI
ARVCHAHPTL SEAFREANLA ASFGKPINF


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
EIAAB11373 Canis familiaris,Canis lupus familiaris,Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,Dog
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
LF-PA40331 anti-Dihydrolipoamide Dehydrogenase (DLD), Rabbit polyclonal to Dihydrolipoamide Dehydrogenase (DLD), Isotype IgG, Host Rabbit 50 ul
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
CSB-EL006928DO Dog Dihydrolipoyl dehydrogenase, mitochondrial(DLD) ELISA kit 96T
ER555 Dihydrolipoyl dehydrogenase, mitochondrial Elisa Kit 96T
CSB-EL006928RA Rat Dihydrolipoyl dehydrogenase, mitochondrial(DLD) ELISA kit 96T
CSB-EL006928RA Rat Dihydrolipoyl dehydrogenase, mitochondrial(DLD) ELISA kit SpeciesRat 96T
CSB-EL006928DO Dog Dihydrolipoyl dehydrogenase, mitochondrial(DLD) ELISA kit SpeciesDog 96T
CSB-EL006928HU Human Dihydrolipoyl dehydrogenase, mitochondrial(DLD) ELISA kit 96T
CSB-EL006928PI Pig Dihydrolipoyl dehydrogenase, mitochondrial(DLD) ELISA kit SpeciesPig 96T
CSB-EL006928MO Mouse Dihydrolipoyl dehydrogenase, mitochondrial(DLD) ELISA kit 96T
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
CSB-EL006928MO Mouse Dihydrolipoyl dehydrogenase, mitochondrial(DLD) ELISA kit SpeciesMouse 96T
CSB-EL006928HU Human Dihydrolipoyl dehydrogenase, mitochondrial(DLD) ELISA kit SpeciesHuman 96T
DLDH_HUMAN ELISA Kit FOR Dihydrolipoyl dehydrogenase, mitochondrial; organism: Human; gene name: DLD 96T
DLDH_MOUSE ELISA Kit FOR Dihydrolipoyl dehydrogenase, mitochondrial; organism: Mouse; gene name: Dld 96T
EIAAB28681 Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex,Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial,Dlat,Mouse,Mus m


 

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