The Isolation and Primary Structure of a Peptide Containing the Oxidation-Reduction Active Cystine of Escherichia coli Lipoamide Dehydrogenase

Burleigh, Bruce D.; Williams, Charles H.

doi:10.1016/s0021-9258(19)45492-6

Cited by 40 publications

(3 citation statements)

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“…The identification of the COOH-terminal Ser-Lys of the mercuric reductase sequence is based on the amino acid composition and the DNA sequence (Brown et al, 1983); the identification of Asn rather than Asx is also based on the DNA sequence. The sequences shown for glutathione reductase and lipoamide dehydrogenase were determined from enzyme isolated from human erythrocytes (Untucht-Grau et al, 1981) and E. coli (Brown & Perham, 1972; Burleigh & Williams, 1972), respectively. In lipoamide dehydrogenase from pig heart, Val-6 is replaced by Thr (Matthews et al, 1974).…”

Section: Discussionmentioning

confidence: 99%

“…This combination of redox centers is found in a few other flavoproteins as well, including glutathione reductase (EC 1.6.4.2) and lipoamide dehydrogenase (EC 1.6.4.3) (Williams, 1976). These latter two enzymes possess extensive sequence homology (Williams et al, 1982), most notably in the active site region, where the amino acids surrounding the redox-active cysteine residues are highly conserved (Jones & Williams, 1975; Krohne-Ehrich et al, 1977;Matthews et al, 1974;Brown & Perham, 1972; Burleigh & Williams, 1972). Mercuric reductase has recently been shown to share many spectrophotometric, physical, and kinetic properties with glutathione reductase and lipoamide dehydrogenase (Fox & Walsh, 1982).…”

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confidence: 97%

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Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide

Fox¹,

Walsh²

1983

Biochemistry

139

108

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The flavoprotein mercuric reductase encoded on the transposon Tn501 from Pseudomonas aeruginosa has previously been shown to contain a redox-active cystine at the active site and to share many spectrophotometric, physical, and kinetic properties with the nicotinamide disulfide oxidoreductases [Fox, B., & Walsh, C. T. (1982) J. Biol. Chem. 257, 2498-2503], Oxidized mercuric reductase was unreactive toward iodo[l4C] acetamide, yet the two-electron-reduced form, in which the thiols of the redox-active cystine are free, reacted to give a monoalkylated derivative. The major 14C-labeled peptide from a tryptic digestion of labeled mercuric reductase was purified by high-performance liquid chromatography. The partial amino acid sequence of this peptide is Gly-Thr-Ile-Gly-Gly-Thr-SCMC-Val-Asx-Val-Gly-SCMC-Val-Pro.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 97%

Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide

Fox¹,

Walsh²

1983

Biochemistry

139

108

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“…The occurrence of electron transfer between flavin and lipoic acids also is consistent with the calculated distances. A cystine residue participates directly in the electron-transfer reaction in pig heart lipoamide dehydrogenase (Burleigh & Williams, 1972;Massey, 1963). The three-dimensional structure of glutathione reductase, which has an active center and mechanistic homologies with lipoamide dehydrogenase (Williams et al, 1976), has been determined (Zappe et al, 1977).…”

Section: Discussionmentioning

confidence: 99%

Fluorescence studies of the pyruvate dehydrogenase multienzyme complex from Escherichia coli

Angelides¹,

Hammes²

1979

Biochemistry

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Regeneration of the antioxidant ubiquinol by lipoamide dehydrogenase, thioredoxin reductase and glutathione reductase

et al. 2003

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Ubiquinol is a powerful antioxidant, which is oxidized in action and needs to be replaced or regenerated to be capable of a sustained effort. This article summarises current knowledge of extramitochondrial reduction of ubiquinone by three flavoenzymes, i.e. lipoamide dehydrogenase, glutathione reductase and thioredoxin reductase, belonging to the same pyridine nucleotide-disulfide oxidoreductase family. These three enzymes are the most efficient extramitochondrial ubiquinone reductases so far described. The reduction of ubiquinone by lipoamide dehydrogenase and glutathione reductase is potently stimulated by zinc and the highest rate of reduction is achieved at acidic pH and the rates are equal with either NADPH or NADH as co-factors. The most efficient ubiquinone reductases are mammalian cytosolic thioredoxin reductases, which are selenoenzymes with a number of biological functions. Reduction of ubiquinone by thioredoxin reductase is in contrast to the other two enzymes investigated, inhibited by zinc and shows a sharp physiological pH optimum at pH 7.5. Furthermore, the reaction is selenium dependent as revealed from experiments using truncated and mutant forms of the enzyme and also in a cellular context by selenium treatment of transfected thioredoxin reductase overexpressing stable cell lines. The reduction of ubiquinone by the three enzymes offers a multifunctional system for extramitochondrial regeneration of an important antioxidant.

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The Isolation and Primary Structure of a Peptide Containing the Oxidation-Reduction Active Cystine of Escherichia coli Lipoamide Dehydrogenase

Cited by 40 publications

References 32 publications

Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide

Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide

Fluorescence studies of the pyruvate dehydrogenase multienzyme complex from Escherichia coli

Regeneration of the antioxidant ubiquinol by lipoamide dehydrogenase, thioredoxin reductase and glutathione reductase

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