Modular polyketide synthase ketosynthases collaborate with upstream dehydratases to install double bonds.

Ray, Katherine A; Saif, Nisha; Keatinge-Clay, Adrian T

Ray, Katherine A; Saif, Nisha; Keatinge-Clay, Adrian T.

Afiliação

Ray KA; Department of Molecular Biosciences, The University of Texas at Austin, 100 E. 24th St., Austin, TX 78712, USA. adriankc@utexas.edu.
Saif N; Department of Molecular Biosciences, The University of Texas at Austin, 100 E. 24th St., Austin, TX 78712, USA. adriankc@utexas.edu.
Keatinge-Clay AT; Department of Molecular Biosciences, The University of Texas at Austin, 100 E. 24th St., Austin, TX 78712, USA. adriankc@utexas.edu.

Chem Commun (Camb) ; 60(66): 8712-8715, 2024 Aug 13.

Article em En | MEDLINE | ID: mdl-39056119

ABSTRACT

ABSTRACT

A VMYH motif was determined to help ketosynthases in polyketide assembly lines select α,ß-unsaturated intermediates from an equilibrium mediated by an upstream dehydratase. Alterations of this motif decreased ketosynthase selectivity within a model tetraketide synthase, most significantly when replaced by the TNGQ motif of ketosynthases that accept D-ß-hydroxy intermediates.

Assuntos

Hidroliases; Policetídeo Sintases; Policetídeo Sintases/metabolismo; Policetídeo Sintases/química; Hidroliases/metabolismo; Hidroliases/química

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Policetídeo Sintases / Hidroliases Idioma: En Revista: Chem Commun (Camb) Ano de publicação: 2024 Tipo de documento: Article

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