PMID:8380170
Citation |
Akiyama, M, Crooke, E and Kornberg, A (1993) An exopolyphosphatase of Escherichia coli. The enzyme and its ppx gene in a polyphosphate operon. J. Biol. Chem. 268:633-9 |
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Abstract |
A gene, ppx, that encodes a novel exopolyphosphatase of 513 amino acids (58,133 Da) was found downstream of the gene for polyphosphate kinase, ppk. Transcription of the ppx gene depends on the ppk promoters, indicating a polyphosphate (polyP) operon of ppk and ppx. Exopolyphosphatase, purified to homogeneity from overproducing cells, is judged to be a dimer of 58-kDa subunits. Orthophosphate is released processively from the ends of polyP approximately 500 residues long, but chains of approximately 15 residues compete poorly with polyP as substrate; ATP is not a substrate. Mg2+ (1 mM) and a high concentration of K+ (175 mM) support optimal activity. |
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Keywords |
Acid Anhydride Hydrolases; Amino Acid Sequence; Base Sequence; Chromatography, Ion Exchange; DNA, Bacterial/genetics; DNA, Bacterial/isolation & purification; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Kinetics; Macromolecular Substances; Magnesium Chloride/pharmacology; Molecular Sequence Data; Operon; Phosphoric Monoester Hydrolases/genetics; Phosphoric Monoester Hydrolases/isolation & purification; Phosphoric Monoester Hydrolases/metabolism; Plasmids; Polyphosphates/metabolism; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Restriction Mapping; Substrate Specificity; Thermodynamics |
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