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Two substrate binding sites in ascorbate peroxidase: the role of arginine 172.

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Title: Two substrate binding sites in ascorbate peroxidase: the role of arginine 172.
Authors: Bursey EH; Departments of Molecular Biology & Biochemistry and Physiology & Biophysics and the Program in Macromolecular Structure, University of California, Irvine 92697-3900, USA., Poulos TL
Source: Biochemistry [Biochemistry] 2000 Jun 27; Vol. 39 (25), pp. 7374-9.
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
Language: English
Journal Info: Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print Cited Medium: Print ISSN: 0006-2960 (Print) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE
Imprint Name(s): Original Publication: Washington, American Chemical Society.
MeSH Terms: Arginine/*metabolism , Peroxidases/*metabolism, Guaiacol/metabolism ; Peroxidases/chemistry ; Peroxidases/genetics ; Ascorbate Peroxidases ; Kinetics ; Models, Molecular ; Mutagenesis ; Protein Conformation ; Substrate Specificity
Abstract: Site-directed mutagenesis has been used to probe the role of Arg172 in ascorbate utilization by ascorbate peroxidase. Arg172 was changed to lysine, glutamine, and asparagine. Although each of these variants retains the ability to utilize guaiacol as a reductant, they exhibit large decreases in their steady-state rates of ascorbate utilization. Spectroscopic, steady-state, and transient-state experiments indicate that these variant proteins are capable of reacting with hydrogen peroxide to form Compound I, but their ability to oxidize ascorbate to form Compound II, and subsequently the resting state, is severely impeded. Results are presented which highlight the importance of Arg172, and a model is proposed to explain its role in ascorbate utilization.
Grant Information: GM42614 United States GM NIGMS NIH HHS
Substance Nomenclature: 6JKA7MAH9C (Guaiacol)
94ZLA3W45F (Arginine)
EC 1.11.1.- (Peroxidases)
EC 1.11.1.11 (Ascorbate Peroxidases)
Entry Date(s): Date Created: 20000620 Date Completed: 20000804 Latest Revision: 20190613
Update Code: 20260130
DOI: 10.1021/bi000446s
PMID: 10858284
Database: MEDLINE
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PubType: Academic Journal
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  Label: Title
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  Data: Two substrate binding sites in ascorbate peroxidase: the role of arginine 172.
– Name: Author
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  Data: <searchLink fieldCode="AU" term="%22Bursey+EH%22">Bursey EH</searchLink>; Departments of Molecular Biology & Biochemistry and Physiology & Biophysics and the Program in Macromolecular Structure, University of California, Irvine 92697-3900, USA.<br /><searchLink fieldCode="AU" term="%22Poulos+TL%22">Poulos TL</searchLink>
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  Data: <searchLink fieldCode="JN" term="%220370623%22">Biochemistry</searchLink> [Biochemistry] 2000 Jun 27; Vol. 39 (25), pp. 7374-9.
– Name: TypePub
  Label: Publication Type
  Group: TypPub
  Data: Journal Article; Research Support, U.S. Gov't, P.H.S.
– Name: Language
  Label: Language
  Group: Lang
  Data: English
– Name: TitleSource
  Label: Journal Info
  Group: Src
  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22American+Chemical+Society%22">American Chemical Society </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>0370623 <i>Publication Model: </i>Print <i>Cited Medium: </i>Print <i>ISSN: </i>0006-2960 (Print) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200062960%22">00062960 </searchLink><i>NLM ISO Abbreviation: </i>Biochemistry <i>Subsets: </i>MEDLINE
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  Label: Imprint Name(s)
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  Data: <i>Original Publication</i>: Washington, American Chemical Society.
– Name: SubjectMESH
  Label: MeSH Terms
  Group: Su
  Data: <searchLink fieldCode="MM" term="%22Arginine%22">Arginine</searchLink>/<searchLink fieldCode="MM" term="%22Arginine+metabolism%22">*metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Peroxidases%22">Peroxidases</searchLink>/<searchLink fieldCode="MM" term="%22Peroxidases+metabolism%22">*metabolism</searchLink><br /><searchLink fieldCode="MH" term="%22Guaiacol%22">Guaiacol</searchLink>/<searchLink fieldCode="MH" term="%22Guaiacol+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Peroxidases%22">Peroxidases</searchLink>/<searchLink fieldCode="MH" term="%22Peroxidases+chemistry%22">chemistry</searchLink> ; <searchLink fieldCode="MH" term="%22Peroxidases%22">Peroxidases</searchLink>/<searchLink fieldCode="MH" term="%22Peroxidases+genetics%22">genetics</searchLink> ; <searchLink fieldCode="MH" term="%22Ascorbate+Peroxidases%22">Ascorbate Peroxidases</searchLink> ; <searchLink fieldCode="MH" term="%22Kinetics%22">Kinetics</searchLink> ; <searchLink fieldCode="MH" term="%22Models%2C+Molecular%22">Models, Molecular</searchLink> ; <searchLink fieldCode="MH" term="%22Mutagenesis%22">Mutagenesis</searchLink> ; <searchLink fieldCode="MH" term="%22Protein+Conformation%22">Protein Conformation</searchLink> ; <searchLink fieldCode="MH" term="%22Substrate+Specificity%22">Substrate Specificity</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Site-directed mutagenesis has been used to probe the role of Arg172 in ascorbate utilization by ascorbate peroxidase. Arg172 was changed to lysine, glutamine, and asparagine. Although each of these variants retains the ability to utilize guaiacol as a reductant, they exhibit large decreases in their steady-state rates of ascorbate utilization. Spectroscopic, steady-state, and transient-state experiments indicate that these variant proteins are capable of reacting with hydrogen peroxide to form Compound I, but their ability to oxidize ascorbate to form Compound II, and subsequently the resting state, is severely impeded. Results are presented which highlight the importance of Arg172, and a model is proposed to explain its role in ascorbate utilization.
– Name: GrantInfo
  Label: Grant Information
  Group: Grant
  Data: GM42614 United States GM NIGMS NIH HHS
– Name: NumberCAS
  Label: Substance Nomenclature
  Group: ID
  Data: 6JKA7MAH9C (Guaiacol)<br />94ZLA3W45F (Arginine)<br />EC 1.11.1.- (Peroxidases)<br />EC 1.11.1.11 (Ascorbate Peroxidases)
– Name: DateEntry
  Label: Entry Date(s)
  Group: Date
  Data: <i>Date Created: </i>20000620 <i>Date Completed: </i>20000804 <i>Latest Revision: </i>20190613
– Name: DateUpdate
  Label: Update Code
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  Data: 20260130
– Name: DOI
  Label: DOI
  Group: ID
  Data: 10.1021/bi000446s
– Name: AN
  Label: PMID
  Group: ID
  Data: 10858284
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=cmedm&AN=10858284
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1021/bi000446s
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 7374
    Subjects:
      – SubjectFull: Guaiacol metabolism
        Type: general
      – SubjectFull: Peroxidases chemistry
        Type: general
      – SubjectFull: Peroxidases genetics
        Type: general
      – SubjectFull: Ascorbate Peroxidases
        Type: general
      – SubjectFull: Kinetics
        Type: general
      – SubjectFull: Models, Molecular
        Type: general
      – SubjectFull: Mutagenesis
        Type: general
      – SubjectFull: Protein Conformation
        Type: general
      – SubjectFull: Substrate Specificity
        Type: general
      – SubjectFull: Arginine metabolism
        Type: general
      – SubjectFull: Peroxidases metabolism
        Type: general
    Titles:
      – TitleFull: Two substrate binding sites in ascorbate peroxidase: the role of arginine 172.
        Type: main
  BibRelationships:
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          Name:
            NameFull: Bursey EH
      – PersonEntity:
          Name:
            NameFull: Poulos TL
    IsPartOfRelationships:
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          Dates:
            – D: 27
              M: 06
              Text: 2000 Jun 27
              Type: published
              Y: 2000
          Identifiers:
            – Type: issn-print
              Value: 0006-2960
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              Value: 39
            – Type: issue
              Value: 25
          Titles:
            – TitleFull: Biochemistry
              Type: main
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