The, enzymic synthesis and degradation of starch. part xx.* the disproportionating enzyme (d-enzyme) of the potato

Stanley Peat, William J. Whelan, W. R. Rees

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40 Citations (Scopus)

Abstract

It is shown that D-enzyme (Nature, 1953, 172, 158) is different from phosphorylase, R-enzyme, and the amylases. It has not yet been possible to separate D-enzyme from Q-enzyme but it is demonstrated that the branching and the disproportionating activity are due to independent enzymes. Evidence is presented which shows that D-enzyme is a transglycosylase, transferring two or more glucose units from a maltodextrin substrate to a suitable acceptor and that, in the transfer, only α-1 : 4-glucosidic links are synthesised. The natural substrates for D-enzyme appear to be the maltodextrins, from maltotriose upwards; neither glucose nor, in all probability, maltose functions as donor substrate. The enzyme is not so selective with respect to the " accepting " molecule. The anomalous position of maltose in this system is discussed.

Original languageEnglish
Pages (from-to)44-53
Number of pages10
JournalJournal of the Chemical Society (Resumed)
StatePublished - Dec 1 1956
Externally publishedYes

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4 alpha-glucanotransferase
Solanum tuberosum
Starch
Degradation
Maltose
Substrates
Enzymes
1,4-alpha-Glucan Branching Enzyme
Glucose
Phosphorylases
Amylases
Molecules

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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