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Escherichia coli Orf135 (NudG) mutant protein specific for oxidized dATP.

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Title: Escherichia coli Orf135 (NudG) mutant protein specific for oxidized dATP.
Authors: Kamiya H; Graduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, Japan.
Source: Nucleosides, nucleotides & nucleic acids [Nucleosides Nucleotides Nucleic Acids] 2025; Vol. 44 (11), pp. 886-893. Date of Electronic Publication: 2024 Oct 11.
Publication Type: Journal Article
Language: English
Journal Info: Publisher: Taylor & Francis Country of Publication: United States NLM ID: 100892832 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1532-2335 (Electronic) Linking ISSN: 15257770 NLM ISO Abbreviation: Nucleosides Nucleotides Nucleic Acids Subsets: MEDLINE
Imprint Name(s): Publication: Philadelphia : Taylor & Francis
Original Publication: Monticello, NY : Marcel Dekker, c2000-
MeSH Terms: Escherichia coli*/genetics , Escherichia coli*/enzymology , Escherichia coli*/metabolism , Pyrophosphatases*/genetics , Pyrophosphatases*/metabolism , Pyrophosphatases*/chemistry , Escherichia coli Proteins*/metabolism , Escherichia coli Proteins*/genetics , Escherichia coli Proteins*/chemistry , Deoxyadenine Nucleotides*/metabolism , Deoxyadenine Nucleotides*/chemistry , Mutant Proteins*/metabolism , Mutant Proteins*/genetics , Mutant Proteins*/chemistry, Oxidation-Reduction ; Substrate Specificity ; Mutation ; Nudix Hydrolases
Abstract: Damaged 2'-deoxyribonucleotides cause mutations, cancer, cell death, and aging. The Escherichia coli Orf135 (NudG) protein catalyzes the hydrolysis of various 2'-deoxyribonucleotides including an oxidized form of dATP, 2-oxo-1,2-dihydro-2'-deoxyadenosine 5'-triphosphate (dAOTP, 2-hydroxy-2'-deoxyadenosine 5'-triphosphate). The best substrate is 5-methyl-2'-deoxycytidine 5'-triphosphate (dCmTP), and the protein prefers dCmTP over dAOTP by ∼200-fold in vitro. To make the enzyme specific for the mutagenic nucleotide dAOTP, a double mutant protein (E33A plus D118E) was designed and produced in E. coli. The purified mutant protein showed one order of magnitude higher dAOTP preference over dCmTP. The split protein based on this mutant may potentially be used to detect dAOTP in living cells.
Contributed Indexing: Keywords: 2-dihydro-2’-deoxyadenosine 5’-triphosphate; 2-oxo-1; 5-methyl-2’-deoxycytidine 5’-triphosphate; NudG; Orf135; substrate specificity
Substance Nomenclature: EC 3.6.1.- (Pyrophosphatases)
0 (Escherichia coli Proteins)
0 (Deoxyadenine Nucleotides)
EC 3.6.1.- (Nudix Hydrolases)
K8KCC8SH6N (2'-deoxyadenosine triphosphate)
0 (Mutant Proteins)
Entry Date(s): Date Created: 20241011 Date Completed: 20250925 Latest Revision: 20250925
Update Code: 20260130
DOI: 10.1080/15257770.2024.2413878
PMID: 39393082
Database: MEDLINE
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  Data: Escherichia coli Orf135 (NudG) mutant protein specific for oxidized dATP.
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  Data: <searchLink fieldCode="AU" term="%22Kamiya+H%22">Kamiya H</searchLink>; Graduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, Japan.
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  Data: <searchLink fieldCode="JN" term="%22100892832%22">Nucleosides, nucleotides & nucleic acids</searchLink> [Nucleosides Nucleotides Nucleic Acids] 2025; Vol. 44 (11), pp. 886-893. <i>Date of Electronic Publication: </i>2024 Oct 11.
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  Data: <i>Publication</i>: Philadelphia : Taylor & Francis<br /><i>Original Publication</i>: Monticello, NY : Marcel Dekker, c2000-
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  Data: <searchLink fieldCode="MM" term="%22Escherichia+coli%22">Escherichia coli*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Escherichia+coli%22">Escherichia coli*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+enzymology%22">enzymology</searchLink> <br /><searchLink fieldCode="MM" term="%22Escherichia+coli%22">Escherichia coli*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Pyrophosphatases%22">Pyrophosphatases*</searchLink>/<searchLink fieldCode="MM" term="%22Pyrophosphatases+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Pyrophosphatases%22">Pyrophosphatases*</searchLink>/<searchLink fieldCode="MM" term="%22Pyrophosphatases+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Pyrophosphatases%22">Pyrophosphatases*</searchLink>/<searchLink fieldCode="MM" term="%22Pyrophosphatases+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Escherichia+coli+Proteins%22">Escherichia coli Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Escherichia+coli+Proteins%22">Escherichia coli Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+Proteins+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Escherichia+coli+Proteins%22">Escherichia coli Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+Proteins+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Deoxyadenine+Nucleotides%22">Deoxyadenine Nucleotides*</searchLink>/<searchLink fieldCode="MM" term="%22Deoxyadenine+Nucleotides+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Deoxyadenine+Nucleotides%22">Deoxyadenine Nucleotides*</searchLink>/<searchLink fieldCode="MM" term="%22Deoxyadenine+Nucleotides+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Mutant+Proteins%22">Mutant Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Mutant+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Mutant+Proteins%22">Mutant Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Mutant+Proteins+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Mutant+Proteins%22">Mutant Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Mutant+Proteins+chemistry%22">chemistry</searchLink><br /><searchLink fieldCode="MH" term="%22Oxidation-Reduction%22">Oxidation-Reduction</searchLink> ; <searchLink fieldCode="MH" term="%22Substrate+Specificity%22">Substrate Specificity</searchLink> ; <searchLink fieldCode="MH" term="%22Mutation%22">Mutation</searchLink> ; <searchLink fieldCode="MH" term="%22Nudix+Hydrolases%22">Nudix Hydrolases</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Damaged 2'-deoxyribonucleotides cause mutations, cancer, cell death, and aging. The Escherichia coli Orf135 (NudG) protein catalyzes the hydrolysis of various 2'-deoxyribonucleotides including an oxidized form of dATP, 2-oxo-1,2-dihydro-2'-deoxyadenosine 5'-triphosphate (dA<superscript>O</superscript>TP, 2-hydroxy-2'-deoxyadenosine 5'-triphosphate). The best substrate is 5-methyl-2'-deoxycytidine 5'-triphosphate (dC<superscript>m</superscript>TP), and the protein prefers dC<superscript>m</superscript>TP over dA<superscript>O</superscript>TP by ∼200-fold in vitro. To make the enzyme specific for the mutagenic nucleotide dA<superscript>O</superscript>TP, a double mutant protein (E33A plus D118E) was designed and produced in E. coli. The purified mutant protein showed one order of magnitude higher dA<superscript>O</superscript>TP preference over dC<superscript>m</superscript>TP. The split protein based on this mutant may potentially be used to detect dA<superscript>O</superscript>TP in living cells.
– Name: SubjectMinor
  Label: Contributed Indexing
  Group:
  Data: <i>Keywords: </i>2-dihydro-2’-deoxyadenosine 5’-triphosphate; 2-oxo-1; 5-methyl-2’-deoxycytidine 5’-triphosphate; NudG; Orf135; substrate specificity
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  Data: EC 3.6.1.- (Pyrophosphatases)<br />0 (Escherichia coli Proteins)<br />0 (Deoxyadenine Nucleotides)<br />EC 3.6.1.- (Nudix Hydrolases)<br />K8KCC8SH6N (2'-deoxyadenosine triphosphate)<br />0 (Mutant Proteins)
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  Data: <i>Date Created: </i>20241011 <i>Date Completed: </i>20250925 <i>Latest Revision: </i>20250925
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  Data: 20260130
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  Data: 10.1080/15257770.2024.2413878
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  Data: 39393082
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RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1080/15257770.2024.2413878
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 886
    Subjects:
      – SubjectFull: Oxidation-Reduction
        Type: general
      – SubjectFull: Substrate Specificity
        Type: general
      – SubjectFull: Mutation
        Type: general
      – SubjectFull: Nudix Hydrolases
        Type: general
      – SubjectFull: Escherichia coli genetics
        Type: general
      – SubjectFull: Escherichia coli enzymology
        Type: general
      – SubjectFull: Escherichia coli metabolism
        Type: general
      – SubjectFull: Pyrophosphatases genetics
        Type: general
      – SubjectFull: Pyrophosphatases metabolism
        Type: general
      – SubjectFull: Pyrophosphatases chemistry
        Type: general
      – SubjectFull: Escherichia coli Proteins metabolism
        Type: general
      – SubjectFull: Escherichia coli Proteins genetics
        Type: general
      – SubjectFull: Escherichia coli Proteins chemistry
        Type: general
      – SubjectFull: Deoxyadenine Nucleotides metabolism
        Type: general
      – SubjectFull: Deoxyadenine Nucleotides chemistry
        Type: general
      – SubjectFull: Mutant Proteins metabolism
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      – SubjectFull: Mutant Proteins genetics
        Type: general
      – SubjectFull: Mutant Proteins chemistry
        Type: general
    Titles:
      – TitleFull: Escherichia coli Orf135 (NudG) mutant protein specific for oxidized dATP.
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            NameFull: Kamiya H
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            – D: 01
              M: 01
              Text: 2025
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              Y: 2025
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            – TitleFull: Nucleosides, nucleotides & nucleic acids
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