Literature DB >> 1657865

dGTP triphosphohydrolase, a unique enzyme confined to members of the family Enterobacteriaceae.

S Quirk1, M J Bessman.   

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.

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Year:  1991        PMID: 1657865      PMCID: PMC209013          DOI: 10.1128/jb.173.21.6665-6669.1991

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  13 in total

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3.  The purification and properties of deoxyguanosine triphosphate triphosphohydrolase from Escherichia coli.

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Journal:  J Biol Chem       Date:  1988-01-25       Impact factor: 5.157

4.  Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-encoding gene (dgt) of Escherichia coli.

Authors:  S Quirk; S K Bhatnagar; M J Bessman
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5.  Location and molecular cloning of the structural gene for the deoxyguanosine triphosphate triphosphohydrolase of Escherichia coli.

Authors:  S Quirk; D Seto; S K Bhatnagar; P Gauss; L Gold; M J Bessman
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8.  Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli.

Authors:  S M Wurgler; C C Richardson
Journal:  Proc Natl Acad Sci U S A       Date:  1990-04       Impact factor: 11.205

9.  Escherichia coli dGTP triphosphohydrolase is inhibited by gene 1.2 protein of bacteriophage T7.

Authors:  H E Huber; B B Beauchamp; C C Richardson
Journal:  J Biol Chem       Date:  1988-09-25       Impact factor: 5.157

10.  A unique deoxyguanosine triphosphatase is responsible for the optA1 phenotype of Escherichia coli.

Authors:  B B Beauchamp; C C Richardson
Journal:  Proc Natl Acad Sci U S A       Date:  1988-04       Impact factor: 11.205

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4.  Characterization of the dnaG locus in Mycobacterium smegmatis reveals linkage of DNA replication and cell division.

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Review 6.  Functions of the gene products of Escherichia coli.

Authors:  M Riley
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7.  Characterization of the deoxynucleotide triphosphate triphosphohydrolase (dNTPase) activity of the EF1143 protein from Enterococcus faecalis and crystal structure of the activator-substrate complex.

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  7 in total

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