Molecular mechanisms of transhydrogenase activity and allosteric regulation in eukaryotic type II PHGDH Ser33

Sebastian Perrone, Javier O. Cifuente, Leonardo Mastrella, Alberto Marina, Beatriz Trastoy, Julia Becker-Kettern, Jean-François Conrotte, Adrià Alcaide-Jiménez, Francisco Corzana, Enrico Glaab, Marcelo E. Guerin, Carole L. Linster · 2026

Read Molecular mechanisms of transhydrogenase activity and allosteric regulation in eukaryotic type II PHGDH Ser33 by Sebastian Perrone, Javier O. Cifuente, Leonardo Mastrella, Alberto Marina, Beatriz Trastoy, Julia Becker-Kettern, Jean-François Conrotte, Adrià Alcaide-Jiménez, Francisco Corzana, Enrico Glaab, Marcelo E. Guerin, Carole L. Linster (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13434204.txt.

Description

Sebastian Perrone and a large team examine Ser33 in 2026, a yeast enzyme that helps make serine, a building block for proteins and cell films. In some life forms this enzyme also makes a second product from a swapped partner molecule. The group asks how the yeast form does both jobs and how serine shuts it down.

Crystal images show the enzyme bound to its helper and to each key molecule in turn. Gene edits, lab rate tests, and computer motion studies pin down which parts grip each molecule. The work also shows how a short end piece tunes control in this enzyme family. The detail aids study of serine paths in health.

Catalog record

CREATORSebastian Perrone, Javier O. Cifuente, Leonardo Mastrella, Alberto Marina, Beatriz Trastoy, Julia Becker-Kettern, Jean-François Conrotte, Adrià Alcaide-Jiménez, Francisco Corzana, Enrico Glaab, Marcelo E. Guerin, Carole L. Linster
YEAR2026
COLLECTIONPAPERS
FORMATTXT
FILE SIZE96938
LICENSEhttps://creativecommons.org/licenses/by/4.0
RIGHTSCC BY
SOURCEEurope PMC

Source: https://europepmc.org/article/MED/PMC13434204

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