Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Various dehydrogenases, reductases, and electron transfer proteins involved in respiratory sulfate reduction by Desulfovibrio gigas have been localized with respect to the periplasmic space, membrane, and cytoplasm. This species was grown on a lactate-sulfate medium, and the distribution of enzyme activities and concentrations of electron transfer components were determined in intact cells, cell fractions prepared with a French press, and lysozyme spheroplasts. A significant fraction of formate dehydrogenase was demonstrated to be localized in the periplasmic space in addition to hydrogenase and some c-type cytochrome. Cytochrome b, menaquinone, fumarate reductase, and nitrite reductase were largely localized on the cytoplasmic membrane. Fumarate reductase was situated on the inner aspect on the membrane, and the nitrite reductase appeared to be transmembraneous. Adenylylsulfate reductase, bisulfite reductase (desulfoviridin), pyruvate dehydrogenase, and succinate dehydrogenase activities were localized in the cytoplasm. Significant amounts of hydrogenase and c-type cytochromes were also detected in the cytoplasm. Growth of D. gigas on a formate-sulfate medium containing acetate resulted in a 10-fold increase in membrane-bound formate dehydrogenase and a doubling of c-type cytochromes. Growth on fumarate with formate resulted in an additional increase in b-type cytochrome compared with lactate-sulfate-grown cells.
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PMID:Localization of dehydrogenases, reductases, and electron transfer components in the sulfate-reducing bacterium Desulfovibrio gigas. 724 92

Formate dehydrogenase and fumarate reductase are involved in the electron transport phosphorylation system of Vibrio succinogenes. The orientation of the active sites of these enzymes in the cytoplasmic membrane of the bacterium was investigated with the aim of elucidating the mechanism of energy transduction. This was done by measuring the accessiblities of the enzymes to substrates, dyes and inhibitors both in cells and in cell-derived particles obtained with the French press. 1. After treatment of the cells with lysozyme and EDTA, followed by fractionation, both enzymes were found exclusively in the membranous fractions, while the periplasmic as well as the cytoplasmic fractions were devoid of both of the enzymic activities. 2. The sites of dye interaction of fumarate reductase were inaccessible to non-permeant dyes in cells, but were fully accessible in French-press particles. The Km for succinate as measured with the permeant methylene blue as acceptor was increased ten fold on lysis of the cells. The Km measured in the particles was similar to that of lysed cells and was not altered by lysis. 3. The rates of formate oxidation in the presence of non-permeant dyes and the Km for formate were unaffected by cell lysis. On lysis of French-press particles, formate oxidation with both permeant and non-permeant acceptors was increased about three fold. The extent of stimulation was not altered by inhibition of the enzymic activities. 4. Succinate oxidation by particles was fully inhibited by 4-chloromercuriphenyl sulfonate whereas that of cells was fully resistant. Formate dehydrogenase in cells was inhibited by 4-diazophenyl sulfonate when added together with formate. This compound also inhibited the enzyme in the particles when given in the absence of a lytic agent or after its addition. However, most of the enzyme remained active if the inhibitor was added before the lytic agent. 5. Fumarate and succinate were actively taken up by the cells from the medium, while formate did not even penetrate through the membrane of the bacteria. 6. It is concluded that the substrate and the dye-reactive sites of formate dehydrogenase face the outside, while those of fumarate reductase face the inside of the cytoplasmic membrane of cells of V. succinogenes. About 70% of the French-press particles were inverted with respect to the substrate and dye sites of the enzymes. The membrane is impermeable to formate and does not contain a specific transporter. The electrogenic liberation of protons on the outisde and the uptake of protons from the cytoplasm of the bacteria, which accompany electron transport, can be explained on the basis of the orientation of the substrate sites of the enzymes without net transport of protons across the membrane.
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PMID:The orientation of the substrate sites of formate dehydrogenase and fumarate reductase in the membrane of Vibrio succinogenes. 735 76