M.C. Pelissier scite author profile

Background:The bacterial ManNAc-6P 2-epimerase (NanE) is essential for sialic acid salvage. Results: Crystal structures of NanE in complex with substrate/product coupled to 1 H NMR kinetics on wild-type and variants elucidate the C2-epimerization mechanism. Conclusion: A single lysine catalyst acts as a one-base mechanism for the C2-epimerization reaction interconverting ManNAc-6P to GlcNAc-6P. Significance: A novel deprotonation/reprotonation mechanism involving a single flexible lysine is described.

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Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate.

Pelissier¹,

Lesley²,

Kühn³

et al. 2010

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M.C. Pelissier

Structural Insights into the Catalytic Mechanism of Bacterial Guanosine-diphospho-d-mannose Pyrophosphorylase and Its Regulation by Divalent Ions

Identification of Xin-repeat proteins as novel ligands of the SH3 domains of nebulin and nebulette and analysis of their interaction during myofibril formation and remodeling

Structural and Functional Characterization of the Clostridium perfringens N-Acetylmannosamine-6-phosphate 2-Epimerase Essential for the Sialic Acid Salvage Pathway

Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate.

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