期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 418, 期 1, 页码 34-38出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0003-9861(03)00341-2
关键词
branching enzyme; glycogen synthesis; starch; branching pattern; alpha-glucan transfer
Truncation of 112 amino acids at the N-terminus (Nd1-112) changes the chain transfer pattern of the Escherichia coli glycogen branching enzyme (GBE) [Arch. Biochem. Biophys. 397 (2002) 279]. We investigated further the role of the N-terminus by engineering other truncated GBEs and analyzing the branching pattern by high-performance anion-exchange chromatography. The wild type GBE transfers mainly chains with a degree of polymerization (d.p.) of 8-14, the Nd1-112 enzyme transfers a greater proportion of chains with higher d.p. 15-20, whereas the 63- and 83-amino acid deleted enzymes had an intermediate pattern of transferred chains (d.p. 10-20). These data showed that a progressive shortening of the N-terminus leads to a gradual increase in the length of the transferred chains, suggesting that the N-terminus provides a support for the glucan substrate during the processes of cleavage and transfer of the alpha-(1-4) glucan chains. (C) 2003 Elsevier Inc. All rights reserved.
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