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Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Fragment)

 DLDH_HYMDI              Reviewed;          53 AA.
P80647;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 1.
25-OCT-2017, entry version 39.
RecName: Full=Dihydrolipoyl dehydrogenase;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
Flags: Fragment;
Hymenolepis diminuta (Rat tapeworm).
Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda;
Cyclophyllidea; Hymenolepididae; Hymenolepis.
NCBI_TaxID=6216;
[1] {ECO:0000305}
PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
TISSUE=Larva {ECO:0000269|PubMed:9030666};
PubMed=9030666; DOI=10.1006/expr.1996.4135;
Walker D.J., Burkhart W., Fioravanti C.F.;
"Hymenolepis diminuta: mitochondrial NADH --> NAD transhydrogenation
and the lipoamide dehydrogenase system.";
Exp. Parasitol. 85:158-167(1997).
-!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
cleavage system as well as of the alpha-ketoacid dehydrogenase
complexes (By similarity). This enzyme has lipoamide dehydrogenase
activity and NADH -> NAD transhydrogenation activity. Also
displays some NADH-ferricyanide reductase and NADPH -> NAD
transydrogenation activities. {ECO:0000250|UniProtKB:P09622,
ECO:0000269|PubMed:9030666}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH. {ECO:0000269|PubMed:9030666}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:P00390};
Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P00390};
-!- ENZYME REGULATION: Lipoamide reduction and the NADH -> NAD
reaction are both completely inhibited by copper and cadmium ions.
{ECO:0000269|PubMed:9030666}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.09 mM for NADH for the NADH -> NAD reaction
{ECO:0000269|PubMed:9030666};
KM=0.18 mM for NADH for the lipoamide dehydrogenase reaction
{ECO:0000269|PubMed:9030666};
KM=0.23 mM for AcPyAD for the NADH -> NAD reaction
{ECO:0000269|PubMed:9030666};
KM=0.51 mM for lipoamide {ECO:0000269|PubMed:9030666};
pH dependence:
Optimum pH is 7.5 for NADH -> NAD transhydrogenation, 6.5 for
lipoamide reduction, 4.5 for NADPH -> NAD transhydrogenation,
and 6.5 for NADH-ferricyanide reduction.
{ECO:0000269|PubMed:9030666};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9030666}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9030666}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
{ECO:0000305}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000255}.
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ProteinModelPortal; P80647; -.
SMR; P80647; -.
Proteomes; UP000046397; Genome Assembly.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
SUPFAM; SSF51905; SSF51905; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond; FAD;
Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Redox-active center;
Reference proteome.
CHAIN 1 >53 Dihydrolipoyl dehydrogenase.
/FTId=PRO_0000311713.
NP_BIND 35 44 FAD. {ECO:0000250|UniProtKB:P00390}.
BINDING 53 53 FAD. {ECO:0000250}.
DISULFID 44 49 Redox-active.
{ECO:0000250|UniProtKB:P00390}.
NON_TER 53 53 {ECO:0000303|PubMed:9030666}.
SEQUENCE 53 AA; 5315 MW; D7C11AE8F2F03D94 CRC64;
LSSGEKDLVV IGSGPGGYVA AIKAAQLGML TVCIEKYPTF GGTCLNVGCI PSK


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