D-lactate dehydrogenase binding in Escherichia coli dld- membrane vesicles reconstituted for active transport

scientific article published on April 1974

D-lactate dehydrogenase binding in Escherichia coli dld- membrane vesicles reconstituted for active transport is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode1974PNAS...71.1461S
P356DOI10.1073/PNAS.71.4.1461
P932PMC publication ID388249
P698PubMed publication ID4598306
P5875ResearchGate publication ID18568497

P50authorHoward Ronald KabackQ1562621
P2093author name stringShort SA
Kohn LD
P2860cites workDansyl-Galactoside, a Fluorescent Probe of Active Transport in Bacterial Membrane VesiclesQ34735510
Reconstitution of D-Lactate-Dependent Transport in Membrane Vesicles from a D-Lactate Dehydrogenase Mutant of Escherichia coliQ35107223
Mutants of Salmonella typhimurium and Escherichia coli pleiotropically defective in active transportQ37500211
Mechanisms of active transport in isolated bacterial membrane vesicles. 8. Valinomycin-induced rubidium transportQ44577527
Mechanisms of active transport in isolated membrane vesicles. II. The mechanism of energy coupling between D-lactic dehydrogenase and beta-galactoside transport in membrane preparations from Escherichia coliQ47738217
Mechanisms of active transport in isolated membrane vesicles. I. The site of energy coupling between D-lactic dehydrogenase and beta-galactoside transport in Escherichia coli membrane vesicles.Q53796676
Mechanisms of active transport in isolated bacterial membrane vesicles. 8. The transport of amino acids by membranes prepared from Escherichia coliQ68652267
Mechanisms of active transport in isolated bacterial membrane vesicles. X. Inactivation of D-lactate dehydrogenase and D-lactate dehydrogenase-coupled transport in Escherichia coli membrane vesicles by an acetylenic substrateQ69223127
Membrane D-lactate dehydrogenase from Escherichia coli. Purification and propertiesQ69267560
Inactivation of a Flavoprotein, Lactate Oxidase, by an Acetylenic SubstrateQ70445229
Mechanisms of active transport in isolated bacterial membrane vesicles. XV. Purification and properties of the membrane-bound D-lactate dehydrogenase from Escherichia coliQ93746930
Vinylglycolic acid. An inactivator of the phosphoenolpyruvate-phosphate transferase system in Escherichia coliQ93754845
P433issue4
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
P304page(s)1461-1465
P577publication date1974-04-01
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleD-lactate dehydrogenase binding in Escherichia coli dld- membrane vesicles reconstituted for active transport
P478volume71

Reverse relations

cites work (P2860)
Q36277768A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli
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Q34177802Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli
Q36283023Effect of Detergents on Galactoside Binding by Melibiose Permeases
Q39771795Energetics and molecular biology of active transport in bacterial membrane vesicles
Q38359073Enzymology of Carbohydrate Transport in Bacteria
Q44318023In vitro synthesis of lactose permease to probe the mechanism of membrane insertion and folding
Q67915514Interaction of the membrane-bound D-lactate dehydrogenase of Escherichia coli with phospholipid vesicles and reconstitution of activity using a spin-labeled fatty acid as an electron acceptor: a magnetic resonance and biochemical study
Q28336640Localization of D-lactate dehydrogenase in native and reconstituted Escherichia coli membrane vesicles
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Q36292097Overproduction and nucleotide sequence of the respiratory D-lactate dehydrogenase of Escherichia coli
Q44241891Probing the mechanism of a membrane transport protein with affinity inactivators
Q38350971Properties of a LacY efflux mutant
Q34256140Reconstitution of D-Lactate Dehydrogenase-Deficient Membrane Vesicles using Fluorine-labeled Components: An Approach to Investigating Protein-Lipid Interactions in Biological Membranes.
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