Abstract
Gene ytkD of Bacillus subtilis, a member of the Nudix hydrolase superfamily, has been cloned and expressed in Escherichia coli. The purified protein has been characterized as a nucleoside triphosphatase active on all of the canonical ribo- and deoxyribonucleoside triphosphates. Whereas all other nucleoside triphosphatase members of the superfamily release inorganic pyrophosphate and the cognate nucleoside monophosphate, YtkD hydrolyses nucleoside triphosphates in a stepwise fashion through the diphosphate to the monophosphate, releasing two molecules of inorganic orthophosphate. Contrary to a previous report, our enzymological and genetic studies indicate that ytkD is not an orthologue of E. coli mutT.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacillus subtilis / enzymology
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Bacillus subtilis / genetics*
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Bacterial Proteins* / chemistry
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Bacterial Proteins* / genetics
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Bacterial Proteins* / isolation & purification
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Bacterial Proteins* / metabolism
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Cloning, Molecular
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Escherichia coli Proteins / genetics
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Genetic Complementation Test
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Molecular Sequence Data
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Nucleoside-Triphosphatase* / chemistry
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Nucleoside-Triphosphatase* / genetics
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Nucleoside-Triphosphatase* / isolation & purification
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Nucleoside-Triphosphatase* / metabolism
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Nudix Hydrolases
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Phosphoric Monoester Hydrolases / genetics
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Pyrophosphatases / chemistry*
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Pyrophosphatases / genetics
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Sequence Analysis, DNA
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Substrate Specificity
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Phosphoric Monoester Hydrolases
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Pyrophosphatases
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mutT protein, E coli
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Nucleoside-Triphosphatase