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Literature summary for 2.4.1.266 extracted from

  • Albesa-Jove, D.; Mendoza, F.; Rodrigo-Unzueta, A.; Gomollon-Bel, F.; Cifuente, J.O.; Urresti, S.; Comino, N.; Gomez, H.; Romero-Garcia, J.; Lluch, J.M.; Sancho-Vaello, E.; Biarnes, X.; Planas, A.; Merino, P.; Masgrau, L.; Guerin, M.E.
    A native ternary complex trapped in a crystal reveals the catalytic mechanism of a retaining glycosyltransferase (2015), Angew. Chem. Int. Ed. Engl., 54, 9898-9902.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme in the presence of the sugar donor UDP-Glc, the acceptor substrate phosphoglycerate, and the divalent cation cofactor forms a native ternary complex. The catalytic mechanism is a front-side substrate-assisted SNi-type reaction Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WMW9
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Mycobacterium tuberculosis ATCC 25618 P9WMW9
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Reaction

Reaction Comment Organism Reaction ID
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate front-side substrate-assisted SNi-type reaction Mycobacterium tuberculosis