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Putative xylose and arabinose reductases in Saccharomyces cerevisiae

Träff, Karin LU ; Jonsson, LJ and Hahn-Hägerdal, Bärbel LU (2002) In Yeast 19(14). p.1233-1241
Abstract
Saccharomyces cerevisiae mutants, in which open reading frames (ORFs) displaying similarity to the aldo-keto reductase GRE3 gene have been deleted, were investigated regarding their ability to utilize xylose and arabinose. Reduced xylitol formation from D-xylose in gre3 mutants of S. cerevisiae suggests that Gre3p is the major D-xylose-reducing enzyme in S. cerevisiae. Cell extracts from the gre3 deletion mutant showed no detectable xylose reductase activity. Decreased arabitol formation from L-arabinose indicates that Gre3p, Ypr1p and the protein encoded by YJR096w are the major arabinose reducers in S. cerevisiae. The ypr1 deletion mutant showed the lowest specific L-arabinose reductase activity in cell extracts, 3.5 mU/mg protein... (More)
Saccharomyces cerevisiae mutants, in which open reading frames (ORFs) displaying similarity to the aldo-keto reductase GRE3 gene have been deleted, were investigated regarding their ability to utilize xylose and arabinose. Reduced xylitol formation from D-xylose in gre3 mutants of S. cerevisiae suggests that Gre3p is the major D-xylose-reducing enzyme in S. cerevisiae. Cell extracts from the gre3 deletion mutant showed no detectable xylose reductase activity. Decreased arabitol formation from L-arabinose indicates that Gre3p, Ypr1p and the protein encoded by YJR096w are the major arabinose reducers in S. cerevisiae. The ypr1 deletion mutant showed the lowest specific L-arabinose reductase activity in cell extracts, 3.5 mU/mg protein compared with 7.4 mU/mg protein for the parental strain with no deletions, and the lowest rate of arabitol formation in vivo. In another set of S. cerevisiae strains, the same ORFs were overexpressed. Increased xylose and arabinose reductase activity was observed in cell extracts for S. cerevisiae overexpressing the GRE3, YPR1 and YJR096w genes. These results, in combination with those obtained with the deletion mutants, suggest that Gre3p, Ypr1p and the protein encoded by YJR096w are capable of xylose and arabinose reduction in S. cerevisiae. Both the D-xylose reductase and the L-arabinose reductase activities exclusively used NADPH as co-factor. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
arabinose, xylitol, xylose reductase, Saccharomyces cerevisiae, xylose, arabinose reductase, arabitol
in
Yeast
volume
19
issue
14
pages
1233 - 1241
publisher
John Wiley & Sons
external identifiers
  • pmid:12271459
  • wos:000178623000004
  • scopus:0036799466
ISSN
1097-0061
DOI
10.1002/yea.913
language
English
LU publication?
yes
id
b5c42fef-380d-4e0d-b06d-e754f1e2186a (old id 325098)
date added to LUP
2007-11-16 11:24:51
date last changed
2017-10-29 04:22:39
@article{b5c42fef-380d-4e0d-b06d-e754f1e2186a,
  abstract     = {Saccharomyces cerevisiae mutants, in which open reading frames (ORFs) displaying similarity to the aldo-keto reductase GRE3 gene have been deleted, were investigated regarding their ability to utilize xylose and arabinose. Reduced xylitol formation from D-xylose in gre3 mutants of S. cerevisiae suggests that Gre3p is the major D-xylose-reducing enzyme in S. cerevisiae. Cell extracts from the gre3 deletion mutant showed no detectable xylose reductase activity. Decreased arabitol formation from L-arabinose indicates that Gre3p, Ypr1p and the protein encoded by YJR096w are the major arabinose reducers in S. cerevisiae. The ypr1 deletion mutant showed the lowest specific L-arabinose reductase activity in cell extracts, 3.5 mU/mg protein compared with 7.4 mU/mg protein for the parental strain with no deletions, and the lowest rate of arabitol formation in vivo. In another set of S. cerevisiae strains, the same ORFs were overexpressed. Increased xylose and arabinose reductase activity was observed in cell extracts for S. cerevisiae overexpressing the GRE3, YPR1 and YJR096w genes. These results, in combination with those obtained with the deletion mutants, suggest that Gre3p, Ypr1p and the protein encoded by YJR096w are capable of xylose and arabinose reduction in S. cerevisiae. Both the D-xylose reductase and the L-arabinose reductase activities exclusively used NADPH as co-factor.},
  author       = {Träff, Karin and Jonsson, LJ and Hahn-Hägerdal, Bärbel},
  issn         = {1097-0061},
  keyword      = {arabinose,xylitol,xylose reductase,Saccharomyces cerevisiae,xylose,arabinose reductase,arabitol},
  language     = {eng},
  number       = {14},
  pages        = {1233--1241},
  publisher    = {John Wiley & Sons},
  series       = {Yeast},
  title        = {Putative xylose and arabinose reductases in Saccharomyces cerevisiae},
  url          = {http://dx.doi.org/10.1002/yea.913},
  volume       = {19},
  year         = {2002},
}