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The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability.

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Title: The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability.
Authors: Khan CA; From the Department of Biochemistry and Structural Biology, UT Health San Antonio, San Antonio, Texas 78229 and., Meisburger SP; the Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853., Ando N; the Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853., Fitzpatrick PF; From the Department of Biochemistry and Structural Biology, UT Health San Antonio, San Antonio, Texas 78229 and fitzpatrickp@uthscsa.edu.
Source: The Journal of biological chemistry [J Biol Chem] 2019 Mar 22; Vol. 294 (12), pp. 4359-4367. Date of Electronic Publication: 2019 Jan 23.
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability.
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  Data: <searchLink fieldCode="AU" term="%22Khan+CA%22">Khan CA</searchLink>; From the Department of Biochemistry and Structural Biology, UT Health San Antonio, San Antonio, Texas 78229 and.<br /><searchLink fieldCode="AU" term="%22Meisburger+SP%22">Meisburger SP</searchLink>; the Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853.<br /><searchLink fieldCode="AU" term="%22Ando+N%22">Ando N</searchLink>; the Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853.<br /><searchLink fieldCode="AU" term="%22Fitzpatrick+PF%22">Fitzpatrick PF</searchLink>; From the Department of Biochemistry and Structural Biology, UT Health San Antonio, San Antonio, Texas 78229 and fitzpatrickp@uthscsa.edu.
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  Data: <searchLink fieldCode="JN" term="%222985121R%22">The Journal of biological chemistry</searchLink> [J Biol Chem] 2019 Mar 22; Vol. 294 (12), pp. 4359-4367. <i>Date of Electronic Publication: </i>2019 Jan 23.
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  Data: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Elsevier+Inc%2E+on+behalf+of+American+Society+for+Biochemistry+and+Molecular+Biology%22">Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>2985121R <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1083-351X (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200219258%22">00219258 </searchLink><i>NLM ISO Abbreviation: </i>J Biol Chem <i>Subsets: </i>MEDLINE
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        Value: 10.1074/jbc.RA118.006477
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      – Code: eng
        Text: English
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        StartPage: 4359
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      – TitleFull: The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability.
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            NameFull: Meisburger SP
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            NameFull: Ando N
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            – D: 22
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              Text: 2019 Mar 22
              Type: published
              Y: 2019
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              Value: 12
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