The mechanism of Q-enzyme action and its influence on the structure of amylopectin

Dov Borovsky; Eric E. Smith; William J. Whelan; Dexter French; Shoichi Kikumoto

doi:10.1016/0003-9861(79)90540-X

The mechanism of Q-enzyme action and its influence on the structure of amylopectin

Dov Borovsky, Eric E. Smith, William J. Whelan, Dexter French, Shoichi Kikumoto

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

53 Scopus citations

Abstract

Q-Enzyme is responsible for the synthesis of the 1,6-branch linkages in amylopectin. Its action on a model amylodextrin containing a single branch linkage has been studied. It is concluded that the enzymic process whereby the branch linkages of amylopectin are synthesized is a random action of the branching enzyme on a complex-possibly a double helix-formed between two 1,4-α-glucan chains. This action pattern predicts a novel arrangement of the units chains in amylopectin.

Original language	English (US)
Pages (from-to)	627-631
Number of pages	5
Journal	Archives of Biochemistry and Biophysics
Volume	198
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(79)90540-X
State	Published - Dec 1979

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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title = "The mechanism of Q-enzyme action and its influence on the structure of amylopectin",

abstract = "Q-Enzyme is responsible for the synthesis of the 1,6-branch linkages in amylopectin. Its action on a model amylodextrin containing a single branch linkage has been studied. It is concluded that the enzymic process whereby the branch linkages of amylopectin are synthesized is a random action of the branching enzyme on a complex-possibly a double helix-formed between two 1,4-α-glucan chains. This action pattern predicts a novel arrangement of the units chains in amylopectin.",

author = "Dov Borovsky and Smith, {Eric E.} and Whelan, {William J.} and Dexter French and Shoichi Kikumoto",

note = "Funding Information: Potato Q-enzyme was prepared and assayed as by Borovsky et al. (2). It is an electrophoretically homog- * Dedicated to Professor Frank Dickens, on the occasion of his eightieth birthday. {\textquoteright} Supported by grants from the United States Public Health Service, National Institutes of Health (AM 12352 to W.J.W. and GM 08822 to D.F.). 3 To whom correspondence should be addressed.",

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AU - Whelan, William J.

AU - French, Dexter

AU - Kikumoto, Shoichi

N1 - Funding Information: Potato Q-enzyme was prepared and assayed as by Borovsky et al. (2). It is an electrophoretically homog- * Dedicated to Professor Frank Dickens, on the occasion of his eightieth birthday. ’ Supported by grants from the United States Public Health Service, National Institutes of Health (AM 12352 to W.J.W. and GM 08822 to D.F.). 3 To whom correspondence should be addressed.

PY - 1979/12

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AB - Q-Enzyme is responsible for the synthesis of the 1,6-branch linkages in amylopectin. Its action on a model amylodextrin containing a single branch linkage has been studied. It is concluded that the enzymic process whereby the branch linkages of amylopectin are synthesized is a random action of the branching enzyme on a complex-possibly a double helix-formed between two 1,4-α-glucan chains. This action pattern predicts a novel arrangement of the units chains in amylopectin.

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The mechanism of Q-enzyme action and its influence on the structure of amylopectin

Abstract

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