Purification and characterization of citrate synthase isoenzymes from Pseudomonas aeruginosa.
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Two native citrate synthases were purified, a hexameric CSI and a dimeric CSII; no gene was identified.
"Chemical cross-linking of the native enzymes with either dimethyl suberimidate or glutaraldehyde followed by electrophoretic analysis by SDS/PAGE showed that CSI is a hexamer and CSII is a dimer."
Systems-Wide Dissection of Organic Acid Assimilation in Pseudomonas aeruginosa Reveals a Novel Path To Underground Metabolism.
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Purified PrpC has both citrate synthase and 2-methylcitrate synthase activity.
"Purified PrpCPa exhibits both citrate synthase activity (with acetyl-CoA as a substrate) and 2-methylcitrate synthase activity (with propionyl-CoA as a substrate)."
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A prpC deletion cannot grow on propionate.
"The 2-methylcitrate synthase mutant (ΔprpC) was unable to grow on propionate as a sole carbon source but displayed no detectable growth deficit on any of the other tested carbon sources."
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PrpC supplies citrate synthase activity in vivo when GltA is absent.
"In the absence of citrate synthase (GltA), Pa can survive because of the low-level basal expression of PrpC, a promiscuous enzyme that also has citrate synthase activity."
Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods