Carlos Moreno-Yruela

Nov 3, 2024 | nature.com | Carlos Moreno-Yruela |Sabrina Schulze |Gottfried J. Palm |Nancy Wang |Dianna Hocking |Leila Jebeli | +5 more

AbstractClassical Zn2+-dependent deac(et)ylases play fundamental regulatory roles in life and are well characterized in eukaryotes regarding their structures, substrates and physiological roles. In bacteria, however, classical deacylases are less well understood. We construct a Generalized Profile (GP) and identify thousands of uncharacterized classical deacylases in bacteria, which are grouped into five clusters.

Nov 3, 2024 | nature.com | Carlos Moreno-Yruela |Sabrina Schulze |Gottfried J. Palm |Nancy Wang |Dianna Hocking |Leila Jebeli | +5 more

AbstractClassical Zn2+-dependent deac(et)ylases play fundamental regulatory roles in life and are well characterized in eukaryotes regarding their structures, substrates and physiological roles. In bacteria, however, classical deacylases are less well understood. We construct a Generalized Profile (GP) and identify thousands of uncharacterized classical deacylases in bacteria, which are grouped into five clusters.

Jul 18, 2024 | nature.com | Di Zhang |Jinjun Gao |Zhijun Zhu |Pankaj K. Singh |Cornelius Rimayi |Carlos Moreno-Yruela | +7 more

AbstractLysine l-lactylation (Kl-la) is a novel protein posttranslational modification (PTM) driven by l-lactate. This PTM has three isomers: Kl-la, N-ε-(carboxyethyl)-lysine (Kce) and d-lactyl-lysine (Kd-la), which are often confused in the context of the Warburg effect and nuclear presence.