Xylose metabolism in <i>Pachysolen tannophilus</i>: purification and properties of xylose reductase

Ditzelmüller, Günther; Kubicek, Christian P.; Wöhrer, W.; Röhr, M.

doi:10.1139/m84-214

Cited by 73 publications

(26 citation statements)

References 22 publications

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“…(46), T. corallina (27), and S. commune (8), which have K m s of 8.0, 7.1, and 5.0 mM, respectively. The K m of the C. magnoliae ER was also similar to the values reported for ADRs from the yeasts P. tannophilus (14) and P. stipitis (49).…”

Section: Discussionsupporting

confidence: 82%

“…Aromatic aldehydes are followed in catalytic effectiveness by aliphatic aldehydes and then sugar aldehydes. This order is similar to those reported for AKRs from various mammals (2, 7) and the yeasts Pichia stipitis (49), Pachysolen tannophilus (14), and S. cerevisiae (24).…”

Section: Vol 69 2003 Er From C Magnoliae 3713supporting

confidence: 88%

“…There are many reports of enzymes that catalyze the formation of glycerol, mannitol, and xylitol, e.g., glyceraldehyde dehydrogenase, mannitol dehydrogenase, and xylose reductase (14,21), respectively, but there are few reports of enzymes that catalyze the formation of erythritol from erythrose. Erythritol is synthesized from erythrose-4-phosphate, an intermediate in the pentose-phosphate pathway, by dephosphorylation and the subsequent reduction of erythrose.…”

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confidence: 99%

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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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Section: Discussionsupporting

confidence: 82%

Section: Vol 69 2003 Er From C Magnoliae 3713supporting

confidence: 88%

mentioning

confidence: 99%

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Purification and Characterization of a Novel Erythrose Reductase from Candida magnoliae

Lee¹,

Kim²,

Ryu

et al. 2003

Appl Environ Microbiol

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“…This result is in accordance with the literature, in so far as the optimum pH for XR activity was 5.5 for Candida guilliermondii (Silva, et al, 1996), 6.0 for Pachysolen tannophylus (Dietzelmuller et al, 1984) and Pichia stipitis (Verduyn et al, 1985). However, the maximum XR activity diminished about 44% after submission to the extraction (Figure 1), probably due to the direct effect of the organic solvent and CTAB on the structure of the enzyme (Kopp, Schede, 2004).…”

Section: Resultssupporting

confidence: 92%

Characterization of xylose reductase extracted by CTAB-reversed micelles from Candida guilliermondii homogenate

Cortez

Pessoa

Felipe³

et al. 2006

Rev. Bras. Cienc. Farm.

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“…Although xylose reductases have been purified from several yeasts (Bolen et al, 1985(Bolen et al, , 1986Ditzelmuller et al, 1984;Ho et al, 1990;Rizzi et al, 1988;Scher & Horecker, 1966;Suzuki & Onishi, 1975;Verduyn et al 1985;Watson et al, 1969) and the amino acid sequence of the P. stipitis xylose reductase has recently been published (Amore et al, 1991;Hallborn et al, 1991;Takuma et al, 1991), little is known about the enzyme's catalytic mechanism or the nature of its catalytic sites. Yeast xylose reductases have been classified as members of the aldose reductase enzyme family (alditol : NAD(P)+ 1-oxidoreductase, EC 1 .…”

Section: Introductionmentioning

confidence: 99%

Characterization of xylose reductase from the yeast Pichia stipitis: Evidence for functional thiol and histidyl groups

Webb

Lee

1992

Journal of General Microbiology

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Xylose reductase (EC 1.1.1.21) from the yeast Pichia stipitis NRC 2548 was purified to homogeneity via a twostep protocol using anion-exchange and gel-filtration chromatography. The pH-activity profile revealed the presence of two ionizable groups with pK,,, values of 5.8 and 8.1, suggesting the catalytic involvement of histidyl and thiol groups, respectively. Additional evidence supporting the involvement of these residues was provided by the use of group-specific inhibitors. The enzyme was rapidly inactivated in a pseudo-first order manner by the thiolspecific modifier p-chloromercuriphenylsulphonate (PMBS) and analysis of the order-of-reaction suggested that one essential cysteine residue was modified to effect inactivation. Treatment of the enzyme with another thiolspecific modifier, 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), showed that modification of one cysteine per monomer led to 90 % loss of activity, further supporting the existence of one essential cysteine residue. Inactivation by PMBS was reversed by adding 1 mM-P-mercaptoethanol. Inactivation of xylose reductase by the histidinespecific modifier diethylpyrocarbonate (DEP) followed a pseudo-first order process, and analysis of the order-ofreaction suggested that one essential histidine residue was modified to effect inactivation. Treatment of DEPinactivated enzyme with 0.2 M-neutral hydroxylamine resulted in the recovery of 45% of enzyme activity. Protection of xylose reductase from PMBS-and DEP-inactivation was provided by NADPH and NADH but not by NADP+, D-XylOSe or Dbglyceraldehyde. This suggests that the essential histidine and cysteine residues may be involved with binding of cofactor by the P(, stipitis xylose reductase.

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Xylose metabolism in Pachysolen tannophilus: purification and properties of xylose reductase

Cited by 73 publications

References 22 publications

Purification and Characterization of a Novel Erythrose Reductase from Candida magnoliae

Purification and Characterization of a Novel Erythrose Reductase from Candida magnoliae

Characterization of xylose reductase extracted by CTAB-reversed micelles from Candida guilliermondii homogenate

Characterization of xylose reductase from the yeast Pichia stipitis: Evidence for functional thiol and histidyl groups

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