Diaphorase Enzyme | DLD enzyme

Diaphorase

Cat. Num. AAA653948

• Gene Names: DLD; E3; LAD; DLDD; DLDH; GCSL; PHE3
• Purity: Molecular Biology Grade
• Synonyms: Diaphorase; DLD enzyme

• Purity/Purification: Molecular Biology Grade

• Preparation and Storage: -20 degree C

Related Product Information for DLD enzyme

The diaphorases are a ubiquitous class of flavin-bound enzymes that catalyze the reduction of various dyes which act as hydrogen acceptors from the reduced form of di-and tri-phosphopyridine nucleotides, i.e., NADH, NADPH. The first such enzyme to be purified was that from heart muscle (Straub 1939). Almost twenty years later heart diaphorase was shown to be identical to lipoyl dehydrogenase (Massey 1958, 1963). Other diaphorases have been described and purified from various bacteria, plants and mammalian organs. Diaphorase activity of a partially purified extract of Clostridium kluyveri cells, originally described as a source of NADH and NADPH oxidase (Ciotti and Kaplan 1957), was observed in this laboratory and its use applied to the coupled, colorimetric determinations of dehydrogenases and ethanol. (Teller 1958). These methods, based on the decolorization of 2,6-dichlorophenolindophenol were improved by the substitution of a tetrazolium dye which becomes chromogenic on reduction. (Brower and Woodbridge 1970; Nachlas et al. 1960).

Product Categories/Family for DLD enzyme

Molecular Biology; MB-Enzymes

NCBI and Uniprot Product Information

• NCBI GI #: 91199540
• NCBI GeneID: 1738
• NCBI Accession #: NP_000099.2
• NCBI GenBank Nucleotide #: NM_000108.3
• UniProt Accession #: P09622; Q14131; Q14167; Q59EV8; Q8WTS4; B2R5X0
• Molecular Weight: 24kD
• NCBI Official Full Name: dihydrolipoyl dehydrogenase, mitochondrial
• NCBI Official Synonym Full Names: dihydrolipoamide dehydrogenase
• NCBI Official Symbol: DLD
• NCBI Official Synonym Symbols: E3; LAD; DLDD; DLDH; GCSL; PHE3
• NCBI Protein Information: dihydrolipoyl dehydrogenase, mitochondrial; diaphorase; lipoamide reductase; lipoamide dehydrogenase; glycine cleavage system L protein; glycine cleavage system protein L; E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex
• UniProt Protein Name: Dihydrolipoyl dehydrogenase, mitochondrial
• Protein Family: Delta-like protein
• UniProt Gene Name: DLD
• UniProt Synonym Gene Names: GCSL; LAD; PHE3
• UniProt Entry Name: DLDH_HUMAN

NCBI Description

This gene encodes 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-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency. [provided by RefSeq, Jul 2008]

Uniprot Description

Function: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.

Catalytic activity: Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactor: Binds 1 FAD per subunit

By similarity.

Subunit structure: Homodimer. Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by non-covalent bonds. Ref.12

Subcellular location: Mitochondrion matrix.

Post-translational modification: Tyrosine phosphorylated

By similarity.

Involvement in disease: Defects in DLD are involved in the development of congenital infantile lactic acidosis.Maple syrup urine disease (MSUD) [MIM:248600]: A metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include 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. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated.Note: The disease is caused by mutations affecting the gene represented in this entry.

Miscellaneous: The active site is a redox-active disulfide bond.

Sequence similarities: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Sequence caution: The sequence BAD92940.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.