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Gene Review:

pox3 - pyruvate oxidase

Lactobacillus plantarum WCFS1

Goffin, P. et al., Quatravaux, S. et al., Wille, G. et al., Nemeria, N. et al.

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Disease relevance of pox3

Involvement of Pyruvate Oxidase Activity and Acetate Production in the Survival of Lactobacillus plantarum during the Stationary Phase of Aerobic Growth [1].

High impact information on pox3

It is shown that, according to circular dichroism spectroscopy, both the 1',4'-iminopyrimidine and the 4'-aminopyrimidine tautomers coexist on the E1 component of human pyruvate dehydrogenase complex and pyruvate oxidase [2].
In addition to the previously characterized pyruvate oxidase PoxB, the Lactobacillus plantarum genome encodes four predicted pyruvate oxidases (PoxC, PoxD, PoxE, and PoxF) [1].
Pyruvate oxidase activity was highly enhanced by oxygen tension and was responsible for H(2)O(2) production after 12 h of culture, whereas lactate oxidase and NADH-dependent lactate dehydrogenase activities were not correlated to metabolite production [3].
Here, we report the X-ray structures of key intermediates in the oxidative decarboxylation of pyruvate, a central reaction in carbon metabolism catalyzed by the ThDP- and flavin-dependent enzyme pyruvate oxidase (POX)3 from Lactobacillus plantarum [4].

References

Involvement of Pyruvate Oxidase Activity and Acetate Production in the Survival of Lactobacillus plantarum during the Stationary Phase of Aerobic Growth. Goffin, P., Muscariello, L., Lorquet, F., Stukkens, A., Prozzi, D., Sacco, M., Kleerebezem, M., Hols, P. Appl. Environ. Microbiol. (2006) [Pubmed]
The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Nemeria, N., Chakraborty, S., Baykal, A., Korotchkina, L.G., Patel, M.S., Jordan, F. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
Examination of Lactobacillus plantarum lactate metabolism side effects in relation to the modulation of aeration parameters. Quatravaux, S., Remize, F., Bryckaert, E., Colavizza, D., Guzzo, J. J. Appl. Microbiol. (2006) [Pubmed]
The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Wille, G., Meyer, D., Steinmetz, A., Hinze, E., Golbik, R., Tittmann, K. Nat. Chem. Biol. (2006) [Pubmed]

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