A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from <it>Aspergillus niger </it>results in a significant increase in affinity for D-sorbitol
<p>Abstract</p> <p>Background</p> <p>L-arabitol dehydrogenase (LAD) and xylitol dehydrogenase (XDH) are involved in the degradation of L-arabinose and D-xylose, which are among the most abundant monosaccharides on earth. Previous data demonstrated that LAD and XDH not o...
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doaj-f2c44978c6a84166ae9df90f797dab502020-11-24T21:34:41ZengBMCBMC Microbiology1471-21802009-08-019116610.1186/1471-2180-9-166A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from <it>Aspergillus niger </it>results in a significant increase in affinity for D-sorbitolRibot CecileRutten LucyTrejo-Aguilar BlancaWösten Han ABde Vries Ronald P<p>Abstract</p> <p>Background</p> <p>L-arabitol dehydrogenase (LAD) and xylitol dehydrogenase (XDH) are involved in the degradation of L-arabinose and D-xylose, which are among the most abundant monosaccharides on earth. Previous data demonstrated that LAD and XDH not only differ in the activity on their biological substrate, but also that only XDH has significant activity on D-sorbitol and may therefore be more closely related to D-sorbitol dehydrogenases (SDH). In this study we aimed to identify residues involved in the difference in substrate specificity.</p> <p>Results</p> <p>Phylogenetic analysis demonstrated that LAD, XDH and SDH form 3 distinct groups of the family of dehydrogenases containing an Alcohol dehydrogenase GroES-like domain (pfam08240) and likely have evolved from a common ancestor. Modelling of LadA and XdhA of the saprobic fungus <it>Aspergillus niger </it>on human SDH identified two residues in LadA (M70 and Y318), that may explain the absence of activity on D-sorbitol. While introduction of the mutation M70F in LadA of <it>A. niger </it>resulted in a nearly complete enzyme inactivation, the Y318F resulted in increased activity for L-arabitol and xylitol. Moreover, the affinity for D-sorbitol was increased in this mutant.</p> <p>Conclusion</p> <p>These data demonstrates that Y318 of LadA contributes significantly to the substrate specificity difference between LAD and XDH/SDH.</p> http://www.biomedcentral.com/1471-2180/9/166 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ribot Cecile Rutten Lucy Trejo-Aguilar Blanca Wösten Han AB de Vries Ronald P |
spellingShingle |
Ribot Cecile Rutten Lucy Trejo-Aguilar Blanca Wösten Han AB de Vries Ronald P A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from <it>Aspergillus niger </it>results in a significant increase in affinity for D-sorbitol BMC Microbiology |
author_facet |
Ribot Cecile Rutten Lucy Trejo-Aguilar Blanca Wösten Han AB de Vries Ronald P |
author_sort |
Ribot Cecile |
title |
A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from <it>Aspergillus niger </it>results in a significant increase in affinity for D-sorbitol |
title_short |
A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from <it>Aspergillus niger </it>results in a significant increase in affinity for D-sorbitol |
title_full |
A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from <it>Aspergillus niger </it>results in a significant increase in affinity for D-sorbitol |
title_fullStr |
A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from <it>Aspergillus niger </it>results in a significant increase in affinity for D-sorbitol |
title_full_unstemmed |
A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from <it>Aspergillus niger </it>results in a significant increase in affinity for D-sorbitol |
title_sort |
single amino acid change (y318f) in the l-arabitol dehydrogenase (lada) from <it>aspergillus niger </it>results in a significant increase in affinity for d-sorbitol |
publisher |
BMC |
series |
BMC Microbiology |
issn |
1471-2180 |
publishDate |
2009-08-01 |
description |
<p>Abstract</p> <p>Background</p> <p>L-arabitol dehydrogenase (LAD) and xylitol dehydrogenase (XDH) are involved in the degradation of L-arabinose and D-xylose, which are among the most abundant monosaccharides on earth. Previous data demonstrated that LAD and XDH not only differ in the activity on their biological substrate, but also that only XDH has significant activity on D-sorbitol and may therefore be more closely related to D-sorbitol dehydrogenases (SDH). In this study we aimed to identify residues involved in the difference in substrate specificity.</p> <p>Results</p> <p>Phylogenetic analysis demonstrated that LAD, XDH and SDH form 3 distinct groups of the family of dehydrogenases containing an Alcohol dehydrogenase GroES-like domain (pfam08240) and likely have evolved from a common ancestor. Modelling of LadA and XdhA of the saprobic fungus <it>Aspergillus niger </it>on human SDH identified two residues in LadA (M70 and Y318), that may explain the absence of activity on D-sorbitol. While introduction of the mutation M70F in LadA of <it>A. niger </it>resulted in a nearly complete enzyme inactivation, the Y318F resulted in increased activity for L-arabitol and xylitol. Moreover, the affinity for D-sorbitol was increased in this mutant.</p> <p>Conclusion</p> <p>These data demonstrates that Y318 of LadA contributes significantly to the substrate specificity difference between LAD and XDH/SDH.</p> |
url |
http://www.biomedcentral.com/1471-2180/9/166 |
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