View in EDS

Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation.

Saved in:
Bibliographic Details
Title: Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation.
Authors: Daubner SC; Department of Biochemistry, Texas A&M University, College Station, Texas 77843-2128, USA., Melendez J, Fitzpatrick PF
Source: Biochemistry [Biochemistry] 2000 Aug 15; Vol. 39 (32), pp. 9652-61.
Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
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
Database: MEDLINE Ultimate
FullText Text:
  Availability: 0
Header DbId: mdl
DbLabel: MEDLINE Ultimate
An: 10933781
AccessLevel: 2
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AU" term="%22Daubner+SC%22">Daubner SC</searchLink>; Department of Biochemistry, Texas A&M University, College Station, Texas 77843-2128, USA.<br /><searchLink fieldCode="AU" term="%22Melendez+J%22">Melendez J</searchLink><br /><searchLink fieldCode="AU" term="%22Fitzpatrick+PF%22">Fitzpatrick PF</searchLink>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%220370623%22">Biochemistry</searchLink> [Biochemistry] 2000 Aug 15; Vol. 39 (32), pp. 9652-61.
– Name: TypePub
  Label: Publication Type
  Group: TypPub
  Data: Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
– 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
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=mdl&AN=10933781
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1021/bi000493k
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 9652
    Titles:
      – TitleFull: Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Daubner SC
      – PersonEntity:
          Name:
            NameFull: Melendez J
      – PersonEntity:
          Name:
            NameFull: Fitzpatrick PF
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 15
              M: 08
              Text: 2000 Aug 15
              Type: published
              Y: 2000
          Identifiers:
            – Type: issn-print
              Value: 0006-2960
          Numbering:
            – Type: volume
              Value: 39
            – Type: issue
              Value: 32
          Titles:
            – TitleFull: Biochemistry
              Type: main
ResultId 1