Interaction of Selenoprotein PA and the Thioredoxin System, Components of the NADPH-dependent Reduction of Glycine in Eubacterium Acidaminophilum and Clostridium Litorale [corrected]

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1991 Oct 1

PMID 1917832

Citations 6

Authors

D Dietrichs

M Meyer

M Rieth

J R Andreesen

Affiliations

Soon will be listed here.

Abstract

Purification of protein PA of the glycine reductase complex from Eubacterium acidaminophilum and Clostridium litorale [corrected] was monitored by a new spectrophotometric assay. The procedure depended on a specific two- to threefold stimulation of a dihydrolipoamide dehydrogenase activity that is elicited by the interaction of a thioredoxin reductase-like flavoprotein and thioredoxin from both organisms. Protein PA isolated from E. acidaminophilum by 75Se labeling and monitoring of the dithioerythritol-dependent glycine reductase activity was identical in its biochemical, structural, and immunological properties to the protein isolated by using the stimulation assay. Proteins PA from both organisms were glycoproteins of Mr about 18,500 and exhibited very similar N-terminal amino acid sequences. Depletion of thioredoxin from crude extracts of E. acidaminophilum totally diminished the NADPH-dependent but not the dithioerythritol-dependent glycine reduction. The former activity could be fully restored by adding thioredoxin. Antibodies raised against the thioredoxin reductase-like flavoprotein or thioredoxin inhibited to a high extent NADPH-dependent but not dithioerythritol-dependent glycine reductase activity. These results indicate the involvement of the thioredoxin system in the electron flow from reduced pyridine nucleotides to glycine reductase.

Citing Articles

Phylogenomic analysis of the family Peptostreptococcaceae (Clostridium cluster XI) and proposal for reclassification of Clostridium litorale (Fendrich et al. 1991) and Eubacterium acidaminophilum (Zindel et al. 1989) as Peptoclostridium litorale....

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First Insights into the Genome of the Amino Acid-Metabolizing Bacterium Clostridium litorale DSM 5388.

Poehlein A, Alghaithi H, Chandran L, Chibani C, Davydova E, Dhamotharan K Genome Announc. 2014; 2(4).

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Isolation of a cytochrome-deficient mutant strain of Sporomusa sphaeroides not capable of oxidizing methyl groups.

Kamlage B, Blaut M J Bacteriol. 1993; 175(10):3043-50.

PMID: 8491723 PMC: 204624. DOI: 10.1128/jb.175.10.3043-3050.1993.

Glycine reductase selenoprotein A is not a glycoprotein: the positive periodic acid-Schiff reagent test is the result of peptide bond cleavage and carbonyl group generation.

Kimura Y, STADTMAN T Proc Natl Acad Sci U S A. 1995; 92(6):2189-93.

PMID: 7892245 PMC: 42449. DOI: 10.1073/pnas.92.6.2189.

Glycine metabolism in anaerobes.

Andreesen J Antonie Van Leeuwenhoek. 1994; 66(1-3):223-37.

PMID: 7747933 DOI: 10.1007/BF00871641.

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