Sequence and analysis of an aldose (xylose) reductase gene from the xylose‐fermenting yeast
            <i>Pachysolen tannophilus</i>

Bolen, Paul L.; Shepherd, Hurley S.

doi:10.1002/(sici)1097-0061(199610)12:13<1367::aid-yea33>3.0.co;2-#

Cited by 27 publications

(22 citation statements)

References 34 publications

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“…Most ALRs also have a strong preference for NADPH over NADH (10). As far as we are aware, no members of the ALR family are specific for NADH only or show a higher affinity for NADH than for NADPH.…”

Section: Discussionmentioning

confidence: 94%

Cloning and Characterization of the xyl1 Gene, Encoding an NADH-Preferring Xylose Reductase from Candida parapsilosis , and Its Functional Expression in Candida tropicalis

Lee¹,

Koo²,

Kim³

2003

Appl Environ Microbiol

111

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Xylose reductase (XR) is a key enzyme in D-xylose metabolism, catalyzing the reduction of D-xylose to xylitol. An NADH-preferring XR was purified to homogeneity from Candida parapsilosis KFCC-10875, and the xyl1 gene encoding a 324-amino-acid polypeptide with a molecular mass of 36,629 Da was subsequently isolated using internal amino acid sequences and 5 and 3 rapid amplification of cDNA ends. The C. parapsilosis XR showed high catalytic efficiency (k cat /K m ‫؍‬ 1.46 s ؊1 mM ؊1 ) for D-xylose and showed unusual coenzyme specificity, with greater catalytic efficiency with NADH (k cat /K m ‫؍‬ 1.39 ؋ 10 4 s ؊1 mM ؊1 ) than with NADPH (k cat /K m ‫؍‬ 1.27 ؋ 10 2 s ؊1 mM ؊1 ), unlike all other aldose reductases characterized. Studies of initial velocity and product inhibition suggest that the reaction proceeds via a sequentially ordered Bi Bi mechanism, which is typical of XRs. Candida tropicalis KFCC-10960 has been reported to have the highest xylitol production yield and rate. It has been suggested, however, that NADPH-dependent XRs, including the XR of C. tropicalis, are limited by the coenzyme availability and thus limit the production of xylitol. The C. parapsilosis xyl1 gene was placed under the control of an alcohol dehydrogenase promoter and integrated into the genome of C. tropicalis. The resulting recombinant yeast, C. tropicalis BN-1, showed higher yield and productivity (by 5 and 25%, respectively) than the wild strain and lower production of by-products, thus facilitating the purification process. The XRs partially purified from C. tropicalis BN-1 exhibited dual coenzyme specificity for both NADH and NADPH, indicating the functional expression of the C. parapsilosis xyl1 gene in C. tropicalis BN-1. This is the first report of the cloning of an xyl1 gene encoding an NADH-preferring XR and its functional expression in C. tropicalis, a yeast currently used for industrial production of xylitol.

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Section: Discussionmentioning

confidence: 94%

Cloning and Characterization of the xyl1 Gene, Encoding an NADH-Preferring Xylose Reductase from Candida parapsilosis , and Its Functional Expression in Candida tropicalis

Lee¹,

Koo²,

Kim³

2003

Appl Environ Microbiol

111

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“…However, a few members of the family can use both cofactors. For example, xylose reductases from the yeasts P. tannophilus (6) and P. stipitis (49), an ADR from the yeast C. tenuis (36), a 3␣-hydroxysteroid dehydrogenase from rat liver (40), and a 3-dehydroecdysone 3␤-reductase cloned from Spodoptera littoralis (9,10) are thought to have dual cofactor specificity. As far as we are aware, no members of the ADR family are specific for NADH only or show higher affinity for NADH than for NADPH.…”

Section: Discussionmentioning

confidence: 99%

“…3. Partial amino acid sequence alignment of ADRs from C. magnoliae (this study), S. cerevisiae (22), K. lactis (3), P. stipitis (1), P. tannophilus (6), and C. tropicalis (54). Identical residues are given against a black background, and similar residues are boxed.…”

Section: Vol 69 2003 Er From C Magnoliae 3713mentioning

confidence: 99%

Purification and Characterization of a Novel Erythrose Reductase from Candida magnoliae

Lee¹,

Kim²,

Ryu

et al. 2003

Appl Environ Microbiol

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Erythritol biosynthesis is catalyzed by erythrose reductase, which converts erythrose to erythritol. Erythrose reductase, however, has never been characterized in terms of amino acid sequence and kinetics. In this study, NAD(P)H-dependent erythrose reductase was purified to homogeneity from Candida magnoliae KFCC 11023 by ion exchange, gel filtration, affinity chromatography, and preparative electrophoresis. The molecular weights of erythrose reductase determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration chromatography were 38,800 and 79,000, respectively, suggesting that the enzyme is homodimeric. Partial amino acid sequence analysis indicates that the enzyme is closely related to other yeast aldose reductases. C. magnoliae erythrose reductase catalyzes the reduction of various aldehydes. Among aldoses, erythrose was the preferred substrate (K m ‫؍‬ 7.9 mM; k cat /K m ‫؍‬ 0.73 mM ؊1 s ؊1 ). This enzyme had a dual coenzyme specificity with greater catalytic efficiency with NADH (k cat /K m ‫؍‬ 450 mM ؊1 s ؊1 ) than with NADPH (k cat /K m ‫؍‬ 5.5 mM ؊1 s ؊1 ), unlike previously characterized aldose reductases, and is specific for transferring the 4-pro-R hydrogen of NADH, which is typical of members of the aldo/keto reductase superfamily. Initial velocity and product inhibition studies are consistent with the hypothesis that the reduction proceeds via a sequential ordered mechanism. The enzyme required sulfhydryl compounds for optimal activity and was strongly inhibited by Cu 2؉ and quercetin, a strong aldose reductase inhibitor, but was not inhibited by aldehyde reductase inhibitors and did not catalyze the reduction of the substrates for carbonyl reductase. These data indicate that the C. magnoliae erythrose reductase is an NAD(P)H-dependent homodimeric aldose reductase with an unusual dual coenzyme specificity.Erythritol, a four-carbon polyol, is widely distributed in nature (16). Like most other polyols, erythritol is a metabolite or storage compound and is found in seaweed, mushrooms, and fruits. It is a noncaloric, noncariogenic sweetener that is safe for diabetics (35). Erythritol has about 70% of the sweetness of sucrose in a 10% (wt/vol) solution and a very high negative heat capacity, providing a strong cooling effect when dissolved (16). Erythritol can be synthesized from dialdehyde starch by a high-temperature chemical reaction in the presence of a nickel catalyst (39). This process has not been industrialized because of its low efficiency. Erythritol also can be produced by microbial methods that utilize osmophilic yeasts and some bacteria (42, 48), and it has been produced commercially by using a mutant of Aureobasidium that produces erythritol in high yield (44% [wt/wt] glucose) (20). Recently, a high-erythritol-producing yeast strain was isolated from honeycombs and the new isolate was identified as Candida magnoliae KFCC 11023 (44). This strain can produce erythritol in high yield (43% [wt/wt] glucose) when cultured appropriately (42, 44).There are many repor...

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“…P. stipitis, P. tannophilus and C. shehatae), D-xylose is converted to D-xylulose by two oxidoreductases in reactions involving the co-factors NAD(P)H and NAD (P) + through the reductase pathway, where D-xylose is initially reduced to xylitol by NAD(P)H-dependent XR [26][27][28][29]. Then xylitol is oxidized to D-xylulose by XDH [26,28,30,31].…”

Section: Sugar Utilizationmentioning

confidence: 99%

Characterization of Bioethanol Production from Hexoses and Xylose by the White Rot Fungus Trametes versicolor

et al. 2011

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Bioethanol production by white rot fungus (Trametes versicolor), identified from fungal mixture in naturally decomposing wood samples, from hexoses and xylose was characterized. Results showed that T. versicolor can grow in culture, under hypoxic conditions, with various mixtures of hexoses and xylose and only xylose. Xylose was efficiently fermented to ethanol in media containing mixtures of hexoses and xylose, such as MBMC and G11XY11 media (Table 1), yielding ethanol concentrations of 20.0 and 9.02 g/l, respectively, after 354 h of hypoxic culture. Very strong correlations were found between ethanolic fermentation (alcohol dehydrogenase activity and ethanol production), sugar consumption and xylose catabolism (xylose reductase, xylitol dehydrogenase and xylulokinase activities) after 354 h in culture in MBMC medium. In a medium (G11XY11) containing a 1:1 glucose/xylose ratio, fermentation efficiency of total sugars into ethanol was 80% after 354 h.

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Sequence and analysis of an aldose (xylose) reductase gene from the xylose‐fermenting yeast Pachysolen tannophilus

Cited by 27 publications

References 34 publications

Cloning and Characterization of the xyl1 Gene, Encoding an NADH-Preferring Xylose Reductase from Candida parapsilosis , and Its Functional Expression in Candida tropicalis

Cloning and Characterization of the xyl1 Gene, Encoding an NADH-Preferring Xylose Reductase from Candida parapsilosis , and Its Functional Expression in Candida tropicalis

Purification and Characterization of a Novel Erythrose Reductase from Candida magnoliae

Characterization of Bioethanol Production from Hexoses and Xylose by the White Rot Fungus Trametes versicolor

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