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Exceptionally versatile take II: post-translational modifications of lysine and their impact on bacterial physiology.
Lassak, Jürgen; Sieber, Alina; Hellwig, Michael.
Afiliación
  • Lassak J; Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Straße 2-4, D-82152 Planegg, Germany.
  • Sieber A; Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Straße 2-4, D-82152 Planegg, Germany.
  • Hellwig M; Technische Universität Braunschweig - Institute of Food Chemistry, Schleinitzstraße 20, D-38106 Braunschweig, Germany.
Biol Chem ; 403(8-9): 819-858, 2022 07 26.
Article en En | MEDLINE | ID: mdl-35172419
ABSTRACT
Among the 22 proteinogenic amino acids, lysine sticks out due to its unparalleled chemical diversity of post-translational modifications. This results in a wide range of possibilities to influence protein function and hence modulate cellular physiology. Concomitantly, lysine derivatives form a metabolic reservoir that can confer selective advantages to those organisms that can utilize it. In this review, we provide examples of selected lysine modifications and describe their role in bacterial physiology.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Lisina Idioma: En Revista: Biol Chem Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Alemania

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Lisina Idioma: En Revista: Biol Chem Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Alemania