Crystal structure of the Glu328Gln mutant of Neisseria polysaccharea amylosucrase in complex with sucrose and maltoheptaose

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Lars K. Skov, Osman Mirza, Desiree Sprogøe, Bart van der Veen, Magali Remaud-Simeon, Cecile Albenne, Pierre Monsan, Michael Gajhede

Several enzymes acting on sucrose are found in glycoside hydrolase family 13 (the α-amylase family). They all transfer a glucosyl moiety from sucrose to an acceptor, but the products can be very different. The structure of a variant of one of these, the Glu328Gln mutant of Neisseria polysaccharea amylosucrase, has been determined in a ternary complex with sucrose and an oligosaccharide to 2.16 Å resolution using x-ray crystallography. Sucrose selectively binds in the active site and the oligosaccharide only binds at surface sites. When this structure is compared to structures of other enzymes acting on sucrose from glycoside hydrolase family 13, it is found that the active site residues are very similar around the glucose part of sucrose while much variation is seen around the fructose moiety.

Original languageEnglish
JournalBiocatalysis and Biotransformation
Volume24
Issue number1-2
Pages (from-to)99-105
Number of pages7
ISSN1024-2422
DOIs
Publication statusPublished - 1 Jan 2006

    Research areas

  • Amylosucrase, Polymerase, Structure/function analysis, Sucrose acting enzymes, Ternary complex

ID: 222546101