Reversal of coenzyme specificity and improvement of catalytic efficiency of Pichiastipitis xylose reductase by rational site-directed mutagenesis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-07

AUTHORS

Qi-Kai Zeng, Hong-Li Du, Jing-Fang Wang, Dong-Qing Wei, Xiao-Ning Wang, Yi-Xue Li, Ying Lin

ABSTRACT

A major problem when xylose is used for ethanol production is the intercellular redox imbalance arising from different coenzyme specificities of xylose reductase (XR) and xylitol dehydrogenase. The residue Lys21 in XR from Pichia stipitis was subjected to site-directed mutagenesis to alter its coenzyme specificity. The N272D mutant exhibited improved catalytic efficiency when NADH was the coenzyme. Both K21A and K21A/N272D preferred NADH to NADPH, their catalytic efficiencies for NADPH were almost zero. The catalytic efficiency of K21A/N272D for NADH was almost 9-fold and 2-fold that of K21A and the wild-type enzyme, respectively. Complete reversal of coenzyme specificity toward NADH and improved catalytic efficiency were achieved. More... »

PAGES

1025-1029

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10529-009-9980-x

DOI

http://dx.doi.org/10.1007/s10529-009-9980-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029105430

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19330484


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