On The Mechanism of Amylose Branching by Potato Q‐Enzyme


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When potato Q‐enzyme converts amylose into an amylopectin‐like molecule, the action is by a random, endo‐type transglycosylation of the substrate chains. Inter‐chain transfer takes place during the formation of the amylopectin branch linkage. This is seen in experiments in which radioactive label was transferred between substrates of disparate molecular weight. Intra‐chain transfer, leading to the formation of a branch linkage, is not excluded by these experiments. The minimum length of amylose chain that can act as an acceptor in the transglycosylation reaction, under the experimental conditions described, is greater than 40 glucose units. The requirement of Q‐enzyme for substrate chains at least 40 glucose units in length is interpreted as meaning that a stabilized secondary and tertiary structure must be established in the substrate before it can be utilized by Q‐enzyme, and that the forces that provide such conformation are sufficiently strong only when the chains are longer than the minimum. Inter‐chain transfer is seen as taking place by one of two mechanisms. The first involves the reaction of the enzyme with a chain that has a stabilized (helical?) conformation. An enzyme‐donor chain intermediate is formed, that then reacts with an acceptor chain to complete the transglycosylation. The second mechanism envisages the substrate for the enzyme as being a complex formed between two chains (a double helix?). The enzyme encounters the complex and carries out an inter‐chain transglycosylation reaction.

Original languageEnglish (US)
Pages (from-to)307-312
Number of pages6
JournalEuropean Journal of Biochemistry
Issue number2
StatePublished - Feb 1976

ASJC Scopus subject areas

  • Biochemistry


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