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Models for the action of barley alpha-amylase isozymes on linear substrates: Carbohydrate Research

โœ 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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๐Ÿ“œ SIMILAR VOLUMES


The action of germinated barley alpha-am
โœ Alex.W. MacGregor; Joan E. Morgan; E.Ann MacGregor ๐Ÿ“‚ Article ๐Ÿ“… 1992 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 915 KB

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

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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