Publications by authors named "Camilla Leogrande"
Article Synopsis
- The thiamine diphosphate (ThDP)-binding motif is crucial for ThDP-dependent enzymes, typically featuring a GDG(X)N sequence, but in the enzyme JanthE, the first glycine is replaced by cysteine (C458).
- JanthE shows high substrate versatility, accepting various long-chain fatty acids and sterically hindered compounds, allowing for the production of different alcohols through carboligation.
- The crystal structure analysis reveals that C458 plays a critical role in maintaining the active site rather than binding the cofactor, and new tetrahedral intermediates with specific substrates were identified, highlighting the enzyme's capabilities in unique carboligation reactions.
The present work aimed to characterize the molecular relationships between structure and function of the seed storage protein β-vignin, the vicilin storage protein of cowpea (, l. Walp) seeds. The molecular characterization of β-vignin was carried out firstly by assessing its thermal stability, under different conditions of pH and ionic strength, by thermal shift assay (TSA) using SYPRO Orange fluorescent dye.
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