dihydrolipoamide dehydrogenase

di·hy·dro·lip·o·am·ide de·hy·dro·gen·ase

(dī-hī'drō-lip-ō-am'id dē-hī'drō-jen-ās'),

A flavoenzyme oxidizing dihydrolipoamide at the expense of NAD⁺; completes the oxidative decarboxylation of pyruvate; a part of several enzyme complexes (for example, α-ketoglutarate dehydrogenase complex). Decreased activity leads to neuronal loss in brain resulting in psychomotor retardation.

Synonym(s): coenzyme factor, lipoamide dehydrogenase, lipoamide reductase (NADH), lipoyl dehydrogenase

Farlex Partner Medical Dictionary © Farlex 2012

dihydrolipoamide dehydrogenase

(di?hi?dro-lip?o-am'id?)

The flavoprotein catalyst of the reoxidation of nicotinamide-adenine dinucleotide (NAD) or nicotinamide-adenine dinucleotide phosphate (NADP) by the mitochondrial electron transport chain. Synonym: diaphorase

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References in periodicals archive ?

In the bacterium Clostridium kluyveri dihydrolipoyl dehydrogenase (synonymously called dihydrolipoamide dehydrogenase) BfmBC reduces Fe(III) complexes of citrate, ATP, and ADP in an NAD(P)H-dependent manner [2].

EsyPred3D also predicted the 3D structure of BfmBC using Geobacillus stearothermophilus dihydrolipoamide dehydrogenase crystal structure (PDB ID 1EBD) as the template (Table 3).

In Thermus scotoductus SA-01 a peripheral membrane-associated protein, identified as a dihydrolipoamide dehydrogenase (LPD) by sequence homology, has been shown to couple NAD(P)H oxidation to Cr(VI) reduction [16].

indiensis LPD1 Geobacillus stearothermophilus dihydrolipoamide dehydrogenase (1EBD) LPD2 Geobacillus stearothermophilus dihydrolipoamide dehydrogenase (1EBD) Trx Escherichia coli thioredoxin reductase (1CL0) NAD(P)H- Novosphingobium aromaticivorans ferredoxin nitrite reductase ArR (3LXD) reductase Tdr Mycobacterium tuberculosis thioredoxin reductase (2A87) Thioredoxin Hyperstable thioredoxin from Precambrian period (2YJ7) Indolepyruvate Pyrococcus furiosus 2-keto acid:ferredoxin ferredoxin oxidoreductase subunit alpha (1YD7) oxidoreductase C.

Identification of multiple soluble Fe(III) reductases in gram-positive thermophilic bacterium Thermoanaerobacter indiensis BSB-33

Forster, "Reversible inactivation of dihydrolipoamide dehydrogenase by Angeli's salt," Acta Biophysica Sinica, vol.

Protein redox modification as a cellular defense mechanism against tissue ischemic injury

Semi-quantitative RT-PCR analysis of dihydrolipoamide dehydrogenase: Total extracted RNA was treated with RQ1 RNase Free DNase (Promega, California, USA) and semi- quantitative RT-PCR performed to analyze the dihydrolipoamide dehydrogenase gene expression.

The extracted RNA using method 1 had high integrity and was successfully used for cDNA synthesis, following the analysis of the differential expression for actin and dihydrolipoamide dehydrogenase genes from salt-treated and non-treated mangrove plants (Figs.

1 was of good quality due to the precise differential expression by dihydrolipoamide dehydrogenase and actin genes during Real time-PCR (Fig.

The present study focuses on dihydrolipoamide dehydrogenase, as an adapted mangrove gene to overcome salt stress effects.

EXTRACTION OF TOTAL RNA FROM MANGROVE PLANTS TO IDENTIFY DIFFERENT GENES INVOLVED IN ITS ADAPTABILITY TO THE VARIETY OF STRESSES