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Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12.

Journal of bacteriology (1988-12-01)
R Lahti, T Pitkäranta, E Valve, I Ilta, E Kukko-Kalske, J Heinonen
RESUMEN

Escherichia coli K-12 gene ppa encoding inorganic pyrophosphatase (PPase) was cloned and sequenced. The 5' end of the ppa mRNA was identified by primer extension mapping. A typical E. coli sigma 70 promoter was identified immediately upstream of the mRNA 5' end. The structural gene of ppa contains 528 base pairs, from which a 175-amino-acid translation product, Mr 19,572, was deduced. The deduced amino acid composition perfectly fitted with that of PPase as previously determined (P. Burton, D. C. Hall, and J. Josse, J. Biol. Chem. 245:4346-4351, 1970). Furthermore, the partial amino acid sequence (residues 1 to 108) of E. coli PPase determined by S. A. Cohen (Ph.D. thesis, University of Chicago, 1978) was the same as that deduced from the nucleotide sequence. This is the first report of the cloning of a PPase gene.

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Sigma-Aldrich
Pyrophosphatase, Inorganic from Escherichia coli, recombinant, expressed in E. coli, lyophilized powder, ≥90%, ≥800 units/mg protein
Sigma-Aldrich
Inorganic Pyrophosphatase from Escherichia coli, ≥100 units/mL, buffered aqueous solution