Potential allosteric sites captured in glycolytic enzymes via residue-based network models: Phosphofructokinase, glyceraldehyde-3-phosphate dehydrogenase and pyruvate kinase.

Celebi, Metehan; Inan, Tugce; Kurkcuoglu, Ozge; Akten, Ebru Demet

Celebi, Metehan; Inan, Tugce; Kurkcuoglu, Ozge; Akten, Ebru Demet.

Celebi M; Graduate Program of Computational Biology and Bioinformatics, Graduate School of Science and Engineering, Kadir Has University, Istanbul, Turkey.
Inan T; Department of Chemical Engineering, Istanbul Technical University, Istanbul, Turkey.
Kurkcuoglu O; Department of Chemical Engineering, Istanbul Technical University, Istanbul, Turkey.
Akten ED; Department of Bioinformatics and Genetics, Faculty of Engineering and Natural Sciences, Kadir Has University, Istanbul, Turkey. Electronic address: demet.akten@khas.edu.tr.

Biophys Chem ; 280: 106701, 2022 01.

Article en En | MEDLINE | ID: mdl-34736071

Asunto(s)

Gliceraldehído-3-Fosfato Deshidrogenasa (Fosforilante); Gliceraldehído-3-Fosfato Deshidrogenasas; Fosfofructoquinasas; Piruvato Quinasa; Regulación Alostérica; Sitio Alostérico; Gliceraldehído-3-Fosfato Deshidrogenasa (Fosforilante)/metabolismo; Gliceraldehído-3-Fosfato Deshidrogenasas/metabolismo; Humanos; Fosfofructoquinasa-1/química; Fosfofructoquinasa-1/metabolismo; Fosfofructoquinasas/metabolismo; Piruvato Quinasa/metabolismo

Palabras clave

Allostery; Communication pathway; Glycolytic; Hub residues; Low-frequency normal mode; Residue network model

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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Piruvato Quinasa / Gliceraldehído-3-Fosfato Deshidrogenasa (Fosforilante) / Fosfofructoquinasas / Gliceraldehído-3-Fosfato Deshidrogenasas Límite: Humans Idioma: En Año: 2022 Tipo del documento: Article

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