The actions of barley alpha-amylase isozymes 1 and 2 (EC 3.2.1.1) on malto-oligosaccharides and theirpnitrophenyl glycosides were similar, but not identical. For each isozyme, transglycosylation occurred with small substrates that were hydrolysed with difficulty, whereas the rates of hydrolysis incr
โฆ LIBER โฆ
Models for the action of barley alpha-amylase isozymes on linear substrates: Carbohydrate Research
โ Scribed by E. Ann MacGregor; Alex W. MacGregor; L.J. Macri; Joan E. Morgan
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 42 KB
- Volume
- 264
- Category
- Article
- ISSN
- 0008-6215
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A model is proposed to explain the action of cereal alpha amylases (EC 3.2.1.1) on such linear substrates as amylose. It is suggested that, at the active site of the enzyme, there are nine contiguous subsites, each capable of interacting with a glucose residue. An estimate is made of the energies in