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Characterization of the branching patterns of glycogen branching enzyme truncated on the N-terminus.

Abstract：

:Truncation of 112 amino acids at the N-terminus (Nd(1-112)) 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 Nd(1-112) 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.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Devillers CH,Piper ME,Ballicora MA,Preiss J

doi

10.1016/s0003-9861(03)00341-2

subject

Has Abstract

pub_date

2003-10-01 00:00:00

pages

34-8

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003986103003412

journal_volume

418

pub_type

杂志文章

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