The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains.

Applied and Environmental Microbiology
Marta PalomoL Dijkhuizen

Abstract

Glycogen branching enzymes (GBE) or 1,4-alpha-glucan branching enzymes (EC 2.4.1.18) introduce alpha-1,6 branching points in alpha-glucans, e.g., glycogen. To identify structural features in GBEs that determine their branching pattern specificity, the Deinococcus geothermalis and Deinococcus radiodurans GBE (GBE(Dg) and GBE(Dr), respectively) were characterized. Compared to other GBEs described to date, these Deinococcus GBEs display unique branching patterns, both transferring relatively short side chains. In spite of their high amino acid sequence similarity (88%) the D. geothermalis enzyme had highest activity on amylose while the D. radiodurans enzyme preferred amylopectin. The side chain distributions of the products were clearly different: GBE(Dg) transferred a larger number of smaller side chains; specifically, DP5 chains corresponded to 10% of the total amount of transferred chains, versus 6.5% for GBE(Dr). GH13-type GBEs are composed of a central (beta/alpha) barrel catalytic domain and an N-terminal and a C-terminal domain. Characterization of hybrid Deinococcus GBEs revealed that the N2 modules of the N domains largely determined substrate specificity and the product branching pattern. The N2 module has recently been...Continue Reading

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Citations

Aug 3, 2011·Die Naturwissenschaften·Liang Wang, Michael J Wise
Jan 23, 2016·Chemical Reviews·Shin-ichiro ShodaShiro Kobayashi
Mar 8, 2013·Carbohydrate Polymers·Jelena Ciric, Katja Loos
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Sep 1, 2018·Comprehensive Reviews in Food Science and Food Safety·Ming MiaoJames N BeMiller
Oct 4, 2021·Comprehensive Reviews in Food Science and Food Safety·Konstantinos KorompokisJan A Delcour

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