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Gene Review:

pflA - pyruvate formate lyase-activating enzyme 1

Escherichia coli O157:H7 str. Sakai

Sauter, M. et al., Young, P. et al., Takahashi-Abbe, S. et al., Wong, K.K. et al.

Takahashi-Abbe, Abe, Takahashi,

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Disease relevance of ECs0985

Transcriptional analysis of the gene encoding pyruvate formate-lyase-activating enzyme of Escherichia coli [1].

High impact information on ECs0985

The homology between the Pfl activating enzyme and T4 55.9 product (in this communication renamed NrdG) in function as well as amino acid sequence is presumably a remnant of an ancient heritage between Pfl and the anaerobic ribonucleotide reductases [2].
The act gene of Escherichia coli encodes the pyruvate formate-lyase-activating enzyme which is necessary for the post-translational modification of pyruvate formate-lyase [1].
The formation of this enzymic radical in vitro requires an activating system composed of PFL-activating enzyme, S-adenosylmethionine, ferrous ion, a reduced flavin, DTT, and pyruvate as an allosteric effector [3].
We have shown that S. mutans has an activating system, including a PFL-activating enzyme (PFL-activase) and an electron transport system; the latter transfers an electron from NADPH to PFL-activase, as occurs in Escherichia coli [4].

References

Transcriptional analysis of the gene encoding pyruvate formate-lyase-activating enzyme of Escherichia coli. Sauter, M., Sawers, R.G. Mol. Microbiol. (1990) [Pubmed]
Bacteriophage T4 gene 55.9 encodes an activity required for anaerobic ribonucleotide reduction. Young, P., Ohman, M., Sjöberg, B.M. J. Biol. Chem. (1994) [Pubmed]
Molecular properties of pyruvate formate-lyase activating enzyme. Wong, K.K., Murray, B.W., Lewisch, S.A., Baxter, M.K., Ridky, T.W., Ulissi-DeMario, L., Kozarich, J.W. Biochemistry (1993) [Pubmed]
Biochemical and functional properties of a pyruvate formate-lyase (PFL)-activating system in Streptococcus mutans. Takahashi-Abbe, S., Abe, K., Takahashi, N. Oral Microbiol. Immunol. (2003) [Pubmed]

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