ArticleThe Biochemical journal2003
Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 70 citations in OpenAlex.
- An NADH/NADApplied and environmental microbiology · 2024Article
- Review
- Structure-function characterization of an aldo-keto reductase involved in detoxification of the mycotoxin, deoxynivalenol.Scientific reports · 2022Article
- Structural Characterization of L-Galactose Dehydrogenase: An Essential Enzyme for Vitamin C Biosynthesis.Plant & cell physiology · 2022Article
- In Vitro and In Silico Approaches for the Evaluation of Antimicrobial Activity, Time-Kill Kinetics, and Anti-Biofilm Potential of Thymoquinone (2-Methyl-5-propan-2-ylcyclohexa-2,5-diene-1,4-dione) against Selected Human Pathogens.Antibiotics (Basel, Switzerland) · 2022Article
- Reductive enzymatic dynamic kinetic resolution affording 115 g/L (S)-2-phenylpropanol.BMC biotechnology · 2021Article
- Characterization of d-xylose reductase, XyrB, fromBiotechnology reports (Amsterdam, Netherlands) · 2021Article
- Genomic and transcriptomic analysis ofBiotechnology for biofuels · 2020Article
- Kinetics and Predicted Structure of a Novel Xylose Reductase fromInternational journal of molecular sciences · 2019Article
- Genome sequence and physiological analysis of Yamadazyma laniorum f.a. sp. nov. and a reevaluation of the apocryphal xylose fermentation of its sister species, Candida tenuis.FEMS yeast research · 2017Article
- A General Tool for Engineering the NAD/NADP Cofactor Preference of Oxidoreductases.ACS synthetic biology · 2017Article
- Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases.The Biochemical journal · 2015Article
- Genetic improvement of native xylose-fermenting yeasts for ethanol production.Journal of industrial microbiology & biotechnology · 2015Review
- Point mutation of the xylose reductase (XR) gene reduces xylitol accumulation and increases citric acid production in Aspergillus carbonarius.Journal of industrial microbiology & biotechnology · 2014Article
- Analysis and prediction of the physiological effects of altered coenzyme specificity in xylose reductase and xylitol dehydrogenase during xylose fermentation by Saccharomyces cerevisiae.Journal of biotechnology · 2012Article
- Increased ethanol productivity in xylose-utilizing Saccharomyces cerevisiae via a randomly mutagenized xylose reductase.Applied and environmental microbiology · 2010Article
- Xylose reductase from the thermophilic fungus Talaromyces emersonii: cloning and heterologous expression of the native gene (Texr) and a double mutant (TexrK271R + N273D) with altered coenzyme specificity.Journal of biosciences · 2009Article
- Computational design of Candida boidinii xylose reductase for altered cofactor specificity.Protein science : a publication of the Protein Society · 2009Article
- Obtaining partial purified xylose reductase from Candida guilliermondii.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2009Article
- Altering the coenzyme preference of xylose reductase to favor utilization of NADH enhances ethanol yield from xylose in a metabolically engineered strain of Saccharomyces cerevisiae.Microbial cell factories · 2008Article
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The co-ordinates reported have been submitted to the Protein Data Bank under accession number 1MI3. Xylose reductase (XR; AKR2B5) is an unusual member of aldo-keto reductase superfamily, because it is one of the few able to efficiently utilize both NADPH and NADH as co-substrates in converting xylose into xylitol. In order to better understand the basis for this dual specificity, we have determined the crystal structure of XR from the yeast Candida tenuis in complex with NAD(+) to 1.80 A resolution (where 1 A=0.1 nm) with a crystallographic R -factor of 18.3%. A comparison of the NAD(+)- and the previously determined NADP(+)-bound forms of XR reveals that XR has the ability to change the conformation of two loops. To accommodate both the presence and absence of the 2'-phosphate, the enzyme is able to adopt different conformations for several different side chains on these loops, including Asn(276), which makes alternative hydrogen-bonding interactions with the adenosine ribose. Also critical is the presence of Glu(227) on a short rigid helix, which makes hydrogen bonds to both the 2'- and 3'-hydroxy groups of the adenosine ribose. In addition to changes in hydrogen-bonding of the adenosine, the ribose unmistakably adopts a 3'- endo conformation rather than the 2'- endo conformation seen in the NADP(+)-bound form. These results underscore the importance of tight adenosine binding for efficient use of either NADH or NADPH as a co-substrate in aldo-keto reductases. The dual specificity found in XR is also an important consideration in designing a high-flux xylose metabolic pathway, which may be improved with an enzyme specific for NADH.
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