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Literature summary for 1.4.1.27 extracted from

  • Steiert, P.S.; Stauffer, L.T.; Stauffer, G.V.
    The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system (1990), J. Bacteriol., 172, 6142-6144 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
acetate the presence of acetate and succinate in the growth medium results in a 50% reduction in inducible GCV enzyme activity Escherichia coli
succinate the presence of acetate and succinate in the growth medium results in a 50% reduction in inducible GCV enzyme activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9P0 i.e. dihydrolipoyl dehydrogenase component LpdA, cf. EC 1.8.1.4
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Synonyms

Synonyms Comment Organism
GCV
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Escherichia coli
LpdA
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Escherichia coli

General Information

General Information Comment Organism
physiological function in an LpdA deletion mutant, inducible GCV enzyme activity is not detected. A D-3-phosphoglycerate dehydrogenase SerA/LpdA double mutant is unable to utilize glycine as a serine source and lacks detectable GCV enzyme activity Escherichia coli