当前位置： SCI文献检索 > ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS期刊下所有文献 > Degradation of the starch components amylopectin and amylose by barley α-amylase 1: role of surface binding site 2.

Degradation of the starch components amylopectin and amylose by barley α-amylase 1: role of surface binding site 2.

Abstract：

:Barley α-amylase isozyme 1 (AMY1, EC 3.2.1.1) contains two surface binding sites, SBS1 and SBS2, involved in the degradation of starch granules. The distinct role of SBS1 and SBS2 remains to be fully understood. Mutational analysis of Tyr-380 situated at SBS2 previously revealed that Tyr-380 is required for binding of the amylose helix mimic, β-cyclodextrin. Also, mutant enzymes altered at position 380 displayed reduced binding to starch granules. Similarly, binding of wild type AMY1 to starch granules was suppressed in the presence of β-cyclodextrin. We investigated the role of SBS2 by comparing kinetic properties of the wild type AMY1 and the Y380A mutant enzyme in hydrolysis of amylopectin, amylose and β-limit dextrin, and the inhibition by β-cyclodextrin. Progress curves of the release of reducing ends revealed a bi-exponential hydrolysis of amylopectin and β-limit dextrin, whereas hydrolysis of amylose progressed mono-exponentially. β-Cyclodextrin, however, inhibited only one of the two reaction rates of amylopectin and β-limit dextrin hydrolysis, whereas hydrolysis of amylose was unaffected. The Y380A enzyme showed no detectable inhibition by β-cyclodextrin but displayed similar kinetics to the inhibited wild type AMY1. These results point to SBS2 as an important binding site in amylopectin depolymerization.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Nielsen JW,Kramhøft B,Bozonnet S,Abou Hachem M,Stipp SL,Svensson B,Willemoës M

doi

10.1016/j.abb.2012.08.005

subject

Has Abstract

pub_date

2012-12-01 00:00:00

pages

1-6

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(12)00304-9

journal_volume

528

pub_type

杂志文章

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