A New Group of Modular Xylanases in Glycoside Hydrolase Family 8 from Marine Bacteria

Applied and Environmental Microbiology
Xiu-Lan ChenPing-Yi Li

Abstract

Xylanases play a crucial role in the degradation of xylan in both terrestrial and marine environments. The endoxylanase XynB from the marine bacterium Glaciecola mesophila KMM 241 is a modular enzyme comprising a long N-terminal domain (NTD) (E44 to T562) with xylan-binding ability and a catalytic domain (CD) (T563 to E912) of glycoside hydrolase family 8 (GH8). In this study, the long NTD is confirmed to contain three different functional regions, which are NTD1 (E44 to D136), NTD2 (Y137 to A193), and NTD3 (L194 to T562). NTD1, mainly composed of eight β-strands, functions as a new type of carbohydrate-binding module (CBM), which has xylan-binding ability but no sequence similarity to any known CBM. NTD2, mainly forming two α-helices, contains one of the α-helices of the catalytic domain's (α/α)6 barrel and therefore is essential for the activity of XynB, although it is far away from the catalytic domain in sequence. NTD3, next to the catalytic domain in sequence, is shown to be helpful in maintaining the thermostability of XynB. Thus, XynB represents a kind of xylanase with a new domain architecture. There are four other predicted glycoside hydrolase sequences with the same domain architecture and high sequence identity (≥80%...Continue Reading

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Citations

Nov 20, 2019·Biochimica Et Biophysica Acta. Proteins and Proteomics·Fatemeh Izadpanah QeshmiKhosro Khajeh
Sep 13, 2021·Journal of the Science of Food and Agriculture·Zhaojun Peng, Yuhong Jin

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