PMID:1657865
| Citation |
Quirk, S and Bessman, MJ (1991) dGTP triphosphohydrolase, a unique enzyme confined to members of the family Enterobacteriaceae. J. Bacteriol. 173:6665-9 |
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| Abstract |
The enzyme dGTP triphosphohydrolase (dGTPase; EC 3.1.5.1) was assayed in partially purified extracts of several genera of bacteria, and it was found to be strictly confined to members of the family Enterobacteriaceae. Whereas 11 of 12 enteric bacteria had comparable activity for this enzyme, 8 of 8 nonenteric bacteria, including species in the very closely related genera Vibrio and Aeromonas, did not assay positively for this enzyme. When challenged with Escherichia coli anti-dGTPase antiserum, the active enzymes fell into three groups, retaining 0, approximately 50, or 100% of their original activity. A computer search has revealed an amino acid sequence in the E. coli enzyme which matches well with the single-stranded-DNA binding motif of Prasad and Chiu (J. Mol. Biol. 193:579-584, 1987) and may account for the enzyme's observed interaction with DNA. As far as we are aware, this is the only enzymatic activity so far reported to be present solely in the enteric bacteria. |
| Links | |
| Keywords |
Amino Acid Sequence; Electrophoresis, Paper; Enterobacteriaceae/enzymology; Eubacterium/enzymology; Molecular Sequence Data; Phosphoric Monoester Hydrolases/immunology; Phosphoric Monoester Hydrolases/metabolism |
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