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Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase

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Standard Standard

Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase. / Xu, Yi-Fan; Lu, Wenyun; Chen, Jonathan C et al.
In: ACS Chemical Biology, Vol. 13, No. 10, 19.10.2018, p. 3011-3020.

Research output: Contribution to journal › Article › peer-review

HarvardHarvard

Xu, Y-F, Lu, W, Chen, JC, Johnson, SA, Gibney, PA, Thomas, DG, Brown, G, May, AL, Campagna, SR, Yakunin, AF, Botstein, D & Rabinowitz, JD 2018, 'Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase', ACS Chemical Biology, vol. 13, no. 10, pp. 3011-3020. https://doi.org/10.1021/acschembio.8b00804

APA

Xu, Y.-F., Lu, W., Chen, J. C., Johnson, S. A., Gibney, P. A., Thomas, D. G., Brown, G., May, A. L., Campagna, S. R., Yakunin, A. F., Botstein, D., & Rabinowitz, J. D. (2018). Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase. ACS Chemical Biology, 13(10), 3011-3020. https://doi.org/10.1021/acschembio.8b00804

CBE

Xu Y-F, Lu W, Chen JC, Johnson SA, Gibney PA, Thomas DG, Brown G, May AL, Campagna SR, Yakunin AF, et al. 2018. Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase. ACS Chemical Biology. 13(10):3011-3020. https://doi.org/10.1021/acschembio.8b00804

MLA

Xu, Yi-Fan et al. "Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase". ACS Chemical Biology. 2018, 13(10). 3011-3020. https://doi.org/10.1021/acschembio.8b00804

VancouverVancouver

Xu YF, Lu W, Chen JC, Johnson SA, Gibney PA, Thomas DG et al. Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase. ACS Chemical Biology. 2018 Oct 19;13(10):3011-3020. Epub 2018 Sept 21. doi: 10.1021/acschembio.8b00804

Author

Xu, Yi-Fan ; Lu, Wenyun ; Chen, Jonathan C et al. / Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase. In: ACS Chemical Biology. 2018 ; Vol. 13, No. 10. pp. 3011-3020.

RIS

TY - JOUR

T1 - Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase

AU - Xu, Yi-Fan

AU - Lu, Wenyun

AU - Chen, Jonathan C

AU - Johnson, Sarah A

AU - Gibney, Patrick A

AU - Thomas, David G

AU - Brown, Greg

AU - May, Amanda L

AU - Campagna, Shawn R

AU - Yakunin, Alexander F

AU - Botstein, David

AU - Rabinowitz, Joshua D

PY - 2018/10/19

Y1 - 2018/10/19

N2 - Sugar alcohols (polyols) exist widely in nature. While some specific sugar alcohol phosphatases are known, there is no known phosphatase for some important sugar alcohols (e.g., sorbitol-6-phosphate). Using liquid chromatography-mass spectrometry-based metabolomics, we screened yeast strains with putative phosphatases of unknown function deleted. We show that the yeast gene YNL010W, which has close homologues in all fungi species and some plants, encodes a sugar alcohol phosphatase. We term this enzyme, which hydrolyzes sorbitol-6-phosphate, ribitol-5-phosphate, and (d)-glycerol-3-phosphate, polyol phosphatase 1 or PYP1. Polyol phosphates are structural analogs of the enediol intermediate of phosphoglucose isomerase (Pgi). We find that sorbitol-6-phosphate and ribitol-5-phosphate inhibit Pgi and that Pyp1 activity is important for yeast to maintain Pgi activity in the presence of environmental sugar alcohols. Pyp1 expression is strongly positively correlated with yeast growth rate, presumably because faster growth requires greater glycolytic and accordingly Pgi flux. Thus, yeast express the previously uncharacterized enzyme Pyp1 to prevent inhibition of glycolysis by sugar alcohol phosphates. Pyp1 may be useful for engineering sugar alcohol production.

AB - Sugar alcohols (polyols) exist widely in nature. While some specific sugar alcohol phosphatases are known, there is no known phosphatase for some important sugar alcohols (e.g., sorbitol-6-phosphate). Using liquid chromatography-mass spectrometry-based metabolomics, we screened yeast strains with putative phosphatases of unknown function deleted. We show that the yeast gene YNL010W, which has close homologues in all fungi species and some plants, encodes a sugar alcohol phosphatase. We term this enzyme, which hydrolyzes sorbitol-6-phosphate, ribitol-5-phosphate, and (d)-glycerol-3-phosphate, polyol phosphatase 1 or PYP1. Polyol phosphates are structural analogs of the enediol intermediate of phosphoglucose isomerase (Pgi). We find that sorbitol-6-phosphate and ribitol-5-phosphate inhibit Pgi and that Pyp1 activity is important for yeast to maintain Pgi activity in the presence of environmental sugar alcohols. Pyp1 expression is strongly positively correlated with yeast growth rate, presumably because faster growth requires greater glycolytic and accordingly Pgi flux. Thus, yeast express the previously uncharacterized enzyme Pyp1 to prevent inhibition of glycolysis by sugar alcohol phosphates. Pyp1 may be useful for engineering sugar alcohol production.

KW - Gene Deletion

KW - Glucose-6-Phosphate Isomerase/antagonists & inhibitors

KW - Hydrolysis

KW - Phosphoric Monoester Hydrolases/genetics

KW - Saccharomyces cerevisiae/enzymology

KW - Saccharomyces cerevisiae Proteins/genetics

KW - Sugar Phosphates/chemistry

U2 - 10.1021/acschembio.8b00804

DO - 10.1021/acschembio.8b00804

M3 - Article

C2 - 30240188

VL - 13

SP - 3011

EP - 3020

JO - ACS Chemical Biology

JF - ACS Chemical Biology

SN - 1554-8929

IS - 10

ER -