EC Number |
Reaction |
Reference |
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2.4.1.25 | maltononaose + maltotriose = maltoundecaose + D-glucose |
catalytic mechanism and domain structure and function |
687741 |
2.4.1.25 | maltononaose + maltotriose = maltoundecaose + D-glucose |
reaction mechanism and catalytic cycle, the catalytic nucleophile changes conformation dramatically during the reaction, Gln256 on the 250s loop is involved in orienting the substrate in the +1 site. The absence of a suitable base in the covalent intermediate structure explains the low hydrolysis activity, overview |
687557 |
2.4.1.25 | maltononaose + maltotriose = maltoundecaose + D-glucose |
this entry covers the former separate entry for EC 2.4.1.3. (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-1,6-glucosidase) |
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