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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)
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author
organization
publishing date
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
2007-06-26 08:20:35
date last changed
2018-05-29 12:18:33
@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},
  volume       = {21},
  year         = {2003},
}