The modular organisation and stability of a thermostable family 10 xylanase
Abou-Hachem, Maher LU ; Olsson, Fredrik LU ; Williamson, M P ; Linse, Sara LU ; Crennell, S J ; Hreggvidsson, G O ; Kristjansson, J K ; Holst, Olle LU and Nordberg Karlsson, Eva LU
(2003)
In Biocatalysis and Biotransformation
21(5-6).
p.253-260
- Abstract
- The thermophilic marine bacterium Rhodothermus marinus produces a modular family 10 xylanase (Xyn10A). It consists of two N-terminal family 4 carbohydrate binding modules (CBMs) followed by a domain of unknown function (D3), and a catalytic module (CM) flanked by a small fifth domain (D5) at its C-terminus. Several truncated mutants of the enzyme have been produced and characterised with respect to biochemical properties and stability. Multiple calcium binding sites are shown to be present in the two N-terminal CBMs and recent evidence suggests that the third domain of the enzyme also has the ability to bind the same metal ligand. The specific binding of Ca2+ was demonstrated to have a pronounced effect on thermostability as shown by... (More)
- The thermophilic marine bacterium Rhodothermus marinus produces a modular family 10 xylanase (Xyn10A). It consists of two N-terminal family 4 carbohydrate binding modules (CBMs) followed by a domain of unknown function (D3), and a catalytic module (CM) flanked by a small fifth domain (D5) at its C-terminus. Several truncated mutants of the enzyme have been produced and characterised with respect to biochemical properties and stability. Multiple calcium binding sites are shown to be present in the two N-terminal CBMs and recent evidence suggests that the third domain of the enzyme also has the ability to bind the same metal ligand. The specific binding of Ca2+ was demonstrated to have a pronounced effect on thermostability as shown by differential scanning calorimetry and thermal inactivation studies. Furthermore, deletion mutants of the enzyme were less stable than the full-length enzyme suggesting that module interactions contributed to the stability of the enzyme. Finally, recent evidence indicates that the fifth domain of Xyn10A is a novel type of module mediating cell-attachment. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/129017
- author
- Abou-Hachem, Maher
LU
; Olsson, Fredrik
LU
; Williamson, M P
; Linse, Sara
LU
; Crennell, S J
; Hreggvidsson, G O
; Kristjansson, J K
; Holst, Olle
LU
and Nordberg Karlsson, Eva
LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biocatalysis and Biotransformation
- volume
- 21
- issue
- 5-6
- pages
- 253 - 260
- publisher
- Taylor & Francis
- external identifiers
-
- wos:000187032500016
- scopus:0347967996
- ISSN
- 1024-2422
- DOI
- 10.1080/1024240310001614315
- language
- English
- LU publication?
- yes
- id
- 9ef23f17-7530-4b4c-bdbe-4f215acca3a7 (old id 129017)
- date added to LUP
- 2016-04-01 12:00:24
- date last changed
- 2025-10-14 11:32:14
@article{9ef23f17-7530-4b4c-bdbe-4f215acca3a7,
abstract = {{The thermophilic marine bacterium Rhodothermus marinus produces a modular family 10 xylanase (Xyn10A). It consists of two N-terminal family 4 carbohydrate binding modules (CBMs) followed by a domain of unknown function (D3), and a catalytic module (CM) flanked by a small fifth domain (D5) at its C-terminus. Several truncated mutants of the enzyme have been produced and characterised with respect to biochemical properties and stability. Multiple calcium binding sites are shown to be present in the two N-terminal CBMs and recent evidence suggests that the third domain of the enzyme also has the ability to bind the same metal ligand. The specific binding of Ca2+ was demonstrated to have a pronounced effect on thermostability as shown by differential scanning calorimetry and thermal inactivation studies. Furthermore, deletion mutants of the enzyme were less stable than the full-length enzyme suggesting that module interactions contributed to the stability of the enzyme. Finally, recent evidence indicates that the fifth domain of Xyn10A is a novel type of module mediating cell-attachment.}},
author = {{Abou-Hachem, Maher and Olsson, Fredrik and Williamson, M P and Linse, Sara and Crennell, S J and Hreggvidsson, G O and Kristjansson, J K and Holst, Olle and Nordberg Karlsson, Eva}},
issn = {{1024-2422}},
language = {{eng}},
number = {{5-6}},
pages = {{253--260}},
publisher = {{Taylor & Francis}},
series = {{Biocatalysis and Biotransformation}},
title = {{The modular organisation and stability of a thermostable family 10 xylanase}},
url = {{http://dx.doi.org/10.1080/1024240310001614315}},
doi = {{10.1080/1024240310001614315}},
volume = {{21}},
year = {{2003}},
}