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Abstract
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.
| Acronyms | ||
| amylosucrase | = | AS |
| glycoside hydrolase | = | GH |
| oligosaccharide binding site | = | OB |
| isomaltulose synthase | = | Pal-I |
| sucrose binding site | = | SB |
| sucrose hydrolase | = | SH |
| sucrose isomerase | = | SI |
| sucrose phosphorylase | = | SP |
| Acronyms | ||
| amylosucrase | = | AS |
| glycoside hydrolase | = | GH |
| oligosaccharide binding site | = | OB |
| isomaltulose synthase | = | Pal-I |
| sucrose binding site | = | SB |
| sucrose hydrolase | = | SH |
| sucrose isomerase | = | SI |
| sucrose phosphorylase | = | SP |