The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system.
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lpdA encodes the glycine cleavage L protein as well as the shared E3 component of pyruvate and 2-oxoglutarate dehydrogenases.
"also functions as the lipoamide dehydrogenase (L protein) in the Escherichia coli glycine cleavage (GCV) enzyme complex"
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Systematic search for zinc-binding proteins in Escherichia coli.
Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase.
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Recombinant E. coli pyruvate dehydrogenase E3 was purified with FAD.
"51,266+/-48Da (E3 including FAD)"
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Purified recombinant 1-lip E2 and E3 were active in an overall PDHc assay.
"purified 1-lip E2 and E3 proteins were functionally active according to the"
Interaction network containing conserved and essential protein complexes in Escherichia coli.
Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth.
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The study assigned detected E. coli proteins to cytosol, periplasm, inner membrane, or outer membrane by biochemical fractionation and tandem MS.
"assigned to the cytosol, periplasm, inner membrane, and outer membrane by biochemical fractionation"
Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes.
Large-scale identification of protein-protein interaction of Escherichia coli K-12.
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex.
Protein abundance profiling of the Escherichia coli cytosol.
The binary protein-protein interaction landscape of Escherichia coli.
Inferring gene function from evolutionary change in signatures of translation efficiency.
Overexpression and mutagenesis of the lipoamide dehydrogenase of Escherichia coli.
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Reconstituted E. coli lpd overexpression increased lipoamide dehydrogenase activity over wild-type levels.
"coli cells transformed with the plasmid carrying the reconstituted lpd gene contained 4-5 times more lipoamide dehydrogenase activity than is normally found in the wild-type organism."
Genetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
Characterization of an Escherichia coli mutant deficient in dihydrolipoyl dehydrogenase activity.
Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and thioredoxin.
2-Oxoacid dehydrogenase complexes of Escherichia coli: cellular amounts and patterns of synthesis.
Cloning and nucleotide sequence of the gcv operon encoding the Escherichia coli glycine-cleavage system.
UniProtKB entry for Escherichia coli LpdA (P0A9P0)