protein

Recombinant Human Dihydrolipoamide Dehydrogenase

MBS143976

0.005 mg

140 USD

Recombinant Protein

Recombinant Human Dihydrolipoamide Dehydrogenase

Dihydrolipoamide Dehydrogenase

DLD Human; Dihydrolipoamide Dehydrogenase Human Recombinant; EC 1.8.1.4; DLD; DLDH; GCSL; PHE3; Dihydrolipoyl dehydrogenase mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; LAD; E3

dihydrolipoyl dehydrogenase, mitochondrial isoform 1; Dihydrolipoyl dehydrogenase, mitochondrial; dihydrolipoyl dehydrogenase, mitochondrial; E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex; diaphorase; glycine cleavage system L protein; glycine cleavage system protein L; lipoamide dehydrogenase; lipoamide reductase; dihydrolipoamide dehydrogenase; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein

DLD

DLD; DLD; E3; LAD; DLDD; DLDH; GCSL; PHE3; GCSL; LAD; PHE3

DLDH_HUMAN

E Coli

509

MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMADQ PIDADVTVIG SGPGGYVAAI KAAQLGFKTV CIEKNETLGG TCLNVGCIPS KALLNNSHYY HMAHGKDFAS RGIEMSEVRL NLDKMMEQKS TAVKALTGGI AHLFKQNKVV HVNGYGKITG KNQVTATKAD GGTQVIDTKN ILIATGSEVT PFPGITIDED TIVSSTGALS LKKVPEKMVV IGAGVIGVEL GSVWQRLGAD VTAVEFLGHV GGVGIDMEIS KNFQRILQKQ GFKFKLNTKV TGATKKSDGK IDVSIEAASG GKAEVITCDV LLVCIGRRPF TKNLGLEELG IELDPRGRIP VNTRFQTKIP NIYAIGDVVA GPMLAHKAED EGIICVEGMA GGAVHIDYNC VPSVIYTHPE VAWVGKSEEQ LKEEGIEYKV GKFPFAANSR AKTNADTDGM VKILGQKSTD RVLGAHILGP GAGEMVNEAA LALEYGASCE DIARVCHAHP TLSEAFREAN LAASFGKSIN F.

Greater than 95% as determined by SDS-PAGE.

The DLD solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol. Sterile Filtered clear colorless solution.

DLD Recombinant Human although stable at 4 degree C for 30 days, should be stored below -20 degree C for periods greater than 30 days. Please avoid freeze-thaw cycles.

ENZYMES; Enzymes; Dehydrogenase

Description: DLD Human Recombinant produced in E Coli is a single, non-glycosylated, polypeptide chain containing 511 amino acids (36-509 a.a.) and having a molecular mass of 54.4 kDa. The DLD is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques. Introduction: DLD is an L protein of the mitochondrial glycine cleavage system which is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. DLD mutations were found in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.

91199540

NP_000099.2

NM_000108.4

P09622

49,283 Da

2-oxobutanoate Degradation Pathway (142413); 2-oxobutanoate Degradation I Pathway (139464); 2-oxoglutarate Decarboxylation To Succinyl-CoA Pathway (142336); 2-oxoglutarate Decarboxylation To Succinyl-CoA Pathway (139119); 2-oxoisovalerate Decarboxylation To Isobutanoyl-CoA Pathway (142335); 2-oxoisovalerate Decarboxylation To Isobutanoyl-CoA Pathway (139118); Branched-chain Amino Acid Catabolism Pathway (106179); Carbon Metabolism Pathway (814926); Carbon Metabolism Pathway (817567); Citrate Cycle (TCA Cycle) Pathway (82927)

This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In homodimeric form, the encoded protein functions as a dehydrogenase and is found in several multi-enzyme complexes that regulate energy metabolism. However, as a monomer, this protein can function as a protease. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]

DLD: a multi-functional mitochondrial enzyme. An enzymatic component of the mitochondrial glycine cleavage system, the pyruvate dehydrogenase complex (PDHC), the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. Is the E3 component of the PDHC that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. The E3 component has dihydrolipoamide dehydrogenase activity. The PDHC contains 20-30 copies of pyruvate decarboxylase tetramers (2 alpha:2 beta)(E1), 60 copies of dihydrolipoamide acetyltransferase (E2), six homodimers of dihydrolipoamide dehydrogenase (E3), plus E3 binding proteins. Defects in DLD are a cause of maple syrup urine disease (MSUD), characterized by mental and physical retardation, feeding problems and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine, resulting from a block in oxidative decarboxylation. Differentially expressed in the Wernicke s Area from patients with schizophrenia. Inhibited by 5-methoxyindole-2-carboxylic acid (MICA). Protein type: EC 1.8.1.4; Oxidoreductase; Mitochondrial; Carbohydrate Metabolism - glycolysis and gluconeogenesis; Carbohydrate Metabolism - citrate (TCA) cycle; Amino Acid Metabolism - valine, leucine and isoleucine degradation; Carbohydrate Metabolism - pyruvate; Amino Acid Metabolism - glycine, serine and threonine. Chromosomal Location of Human Ortholog: 7q31-q32. Cellular Component: nucleoplasm; mitochondrion; mitochondrial matrix; acrosomal matrix; cilium. Molecular Function: mercury (II) reductase activity; FAD binding; mercury ion binding; dihydrolipoyl dehydrogenase activity; NADP binding. Biological Process: mitochondrial electron transport, NADH to ubiquinone; tricarboxylic acid cycle; regulation of acetyl-CoA biosynthetic process from pyruvate; gastrulation; branched chain family amino acid catabolic process; proteolysis; cellular metabolic process; regulation of membrane potential; cell redox homeostasis; detoxification of mercury ion; lysine catabolic process; pyruvate metabolic process; sperm capacitation. Disease: Dihydrolipoamide Dehydrogenase Deficiency

0.005 mg

140 USD

0.025 mg

205

1 mg

2220