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Structure and Catalytic Cycle of beta-1,4-galactosyltransferase

Structure and Catalytic Cycle of beta-1,4-galactosyltransferase

Boopathy Ramakrishnan, Elizabeth Boeggeman, Velavan Ramasamy, Pradman K Qasba

Curr Opin Struct Biol. 2004 Oct;14(5):593-600.

PMID: 15465321

Abstract:

Beta-1,4-galactosyltransferase-1, a housekeeping enzyme that functions in the synthesis of glycoconjugates, has two flexible loops, one short and one long. Upon binding a metal ion and UDP-galactose, the loops change from an open to a closed conformation, repositioning residues to lock the ligands in place. Residues at the N-terminal region of the long loop form the metal-binding site and those at the C-terminal region form a helix, which becomes part of the binding site for the oligosaccharide acceptor; the remaining residues cover the bound sugar-nucleotide. After binding of the oligosaccharide acceptor and transfer of the galactose moiety, the product disaccharide unit is ejected and the enzyme returns to the open conformation, repeating the catalytic cycle.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42410733	Beta-1,4-galactosyltransferase 1			Price

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