Decoupling of catalysis and transition state analog binding from mutations throughout a phosphatase revealed by high-throughput enzymology.

Markin, Craig J; Mokhtari, Daniel A; Du, Siyuan; Doukov, Tzanko; Sunden, Fanny; Cook, Jordan A; Fordyce, Polly M; Herschlag, Daniel

Markin, Craig J; Mokhtari, Daniel A; Du, Siyuan; Doukov, Tzanko; Sunden, Fanny; Cook, Jordan A; Fordyce, Polly M; Herschlag, Daniel.

Afiliação

Markin CJ; Department of Biochemistry, Stanford University, Stanford, CA 94305.
Mokhtari DA; Department of Biochemistry, Stanford University, Stanford, CA 94305.
Du S; Department of Biochemistry, Stanford University, Stanford, CA 94305.
Doukov T; Department of Chemistry, Stanford University, Stanford, CA 94305.
Sunden F; Stanford Synchrotron Radiation Light Source, Stanford Linear Accelerator Centre National Accelerator Laboratory, Menlo Park, CA 94025.
Cook JA; Department of Biochemistry, Stanford University, Stanford, CA 94305.
Fordyce PM; Department of Biochemistry, Stanford University, Stanford, CA 94305.
Herschlag D; ChEM-H Institute, Stanford University, Stanford, CA 94305.

Proc Natl Acad Sci U S A ; 120(29): e2219074120, 2023 07 18.

Article em En | MEDLINE | ID: mdl-37428919

Assuntos

Monoéster Fosfórico Hidrolases; Compostos de Tungstênio; Catálise; Mutação; Cinética; Sítios de Ligação

Palavras-chave

conformational ensembles; enzyme catalysis; high-throughput biochemistry; transition state analogs; transition state specificity

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Compostos de Tungstênio / Monoéster Fosfórico Hidrolases Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2023 Tipo de documento: Article

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