Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system.

Journal of bacteriology - 1 Oct 1990

Steiert P S, Stauffer L T, Stauffer G V

Abstract excerpt

The lpd-encoded lipoamide dehydrogenase, common to the pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes, also functions as the lipoamide dehydrogenase (L protein) in the Escherichia coli glycine cleavage (GCV) enzyme complex. Inducible GCV enzyme activity was not detected in an lpd deletion mutant; lpd+ transductants had normal levels of inducible GCV enzyme activity. A serA lpd double mutant was...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Escherichia coli
Share to Genetic Complementation Test
Share to Genotype

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Mutation

Share to Phenotype

Share to Transferases

Source

Open in PubMed Open full text

Identifiers

PMID: 2211531
DOI: 10.1128/jb.172.10.6142-6144.1990
PMCID: PMC526943

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system.PMID 2211531Read ↗

The Escherichia coli glycine transport system and its role in the regulation of the glycine cleavage enzyme system.Semantic proximity Read ↗

Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein.Semantic proximity Read ↗

Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system.Semantic proximity Read ↗

Characterization of the Escherichia coli gcvR gene encoding a negative regulator of gcv expression.Semantic proximity Read ↗

Lactate racemization as a rescue pathway for supplying D-lactate to the cell wall biosynthesis machinery in Lactobacillus plantarum.Semantic proximity Read ↗

Two roles for the leucine-responsive regulatory protein in expression of the alanine catabolic operon (dadAB) in Klebsiella aerogenes.Semantic proximity Read ↗

The Escherichia coli mutant requiring D-glutamic acid is the result of mutations in two distinct genetic loci.Semantic proximity Read ↗

Roles of the GcvA and PurR proteins in negative regulation of the Escherichia coli glycine cleavage enzyme system.Semantic proximity Read ↗

The Escherichia coli gcvT gene encoding the T-protein of the glycine cleavage enzyme system.Semantic proximity Read ↗

D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation.Semantic proximity Read ↗

GcvR interacts with GcvA to inhibit activation of the Escherichia coli glycine cleavage operon.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.