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Literature summary for 6.4.1.1 extracted from

  • Schaer, J.; Stoll, R.; Schauer, K.; Loeffler, D.I.; Eylert, E.; Joseph, B.; Eisenreich, W.; Fuchs, T.M.; Goebel, W.
    Pyruvate carboxylase plays a crucial role in carbon metabolism of extra- and intracellularly replicating Listeria monocytogenes (2010), J. Bacteriol., 192, 1774-1784.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Listeria monocytogenes
-
-
-
Listeria monocytogenes Sv1/2a EGD-e
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyruvate + HCO3- + H+
-
 Listeria monocytogenes ADP + oxaloacetate + phosphate
-
 ?
ATP + pyruvate + HCO3- + H+
-
 Listeria monocytogenes Sv1/2a EGD-e ADP + oxaloacetate + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
PYC
-
 Listeria monocytogenes
pycA
-
 Listeria monocytogenes

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Listeria monocytogenes

General Information

General Information Comment Organism
malfunction a pycA insertion mutant defective in pyruvate carboxylase still grows, albeit at a reduced rate, in brain heart infusion medium but is unable to multiply in a defined minimal medium with glucose or glycerol as a carbon source. The mutant is also unable to replicate in mammalian cells and exhibits high virulence attenuation in the mouse sepsis model Listeria monocytogenes
metabolism the PYC-catalyzed carboxylation of pyruvate is the predominant reaction leading to oxaloacetate in Listeria monocytogenes Listeria monocytogenes