Escherichia coli Purine Nucleoside Phosphorylase II, the Product of the xapA Gene

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Escherichia coli Purine Nucleoside Phosphorylase II, the Product of the xapA Gene. / Dandanell, Gert; Szczepanowski, R.H.; Kierdaszuk, B.; Shugar, D.; Bochtler, M.

In: Journal of Molecular Biology, Vol. 348, No. 1, 2005, p. 113-25.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Dandanell, G, Szczepanowski, RH, Kierdaszuk, B, Shugar, D & Bochtler, M 2005, 'Escherichia coli Purine Nucleoside Phosphorylase II, the Product of the xapA Gene', Journal of Molecular Biology, vol. 348, no. 1, pp. 113-25. https://doi.org/10.1016/j.jmb.2005.02.019

APA

Dandanell, G., Szczepanowski, R. H., Kierdaszuk, B., Shugar, D., & Bochtler, M. (2005). Escherichia coli Purine Nucleoside Phosphorylase II, the Product of the xapA Gene. Journal of Molecular Biology, 348(1), 113-25. https://doi.org/10.1016/j.jmb.2005.02.019

Vancouver

Dandanell G, Szczepanowski RH, Kierdaszuk B, Shugar D, Bochtler M. Escherichia coli Purine Nucleoside Phosphorylase II, the Product of the xapA Gene. Journal of Molecular Biology. 2005;348(1):113-25. https://doi.org/10.1016/j.jmb.2005.02.019

Author

Dandanell, Gert ; Szczepanowski, R.H. ; Kierdaszuk, B. ; Shugar, D. ; Bochtler, M. / Escherichia coli Purine Nucleoside Phosphorylase II, the Product of the xapA Gene. In: Journal of Molecular Biology. 2005 ; Vol. 348, No. 1. pp. 113-25.

Bibtex

@article{7bdeb80074c311dbbee902004c4f4f50,
title = "Escherichia coli Purine Nucleoside Phosphorylase II, the Product of the xapA Gene",
abstract = "Purine nucleoside phosphorylases (PNPs, E. C. 2.4.2.1) use orthophosphate to cleave the N-glycosidic bond of {\ss}-(deoxy)ribonucleosides to yield a-(deoxy)ribose 1-phosphate and the free purine base. Escherichia coli PNP-II, the product of the xapA gene, is similar to trimeric PNPs in sequence, but has been reported to migrate as a hexamer and to accept xanthosine with comparable efficiency to guanosine and inosine, the usual physiological substrates for trimeric PNPs. Here, we present a detailed biochemical characterization and the crystal structure of E. coli PNP-II. In three different crystal forms, PNP-II trimers dimerize, leading to a subunit arrangement that is qualitatively different from the {"}trimer of dimers{"} arrangement of conventional high molecular mass PNPs. Crystal structures are compatible with similar binding modes for guanine and xanthine, with a preference for the neutral over the monoanionic form of xanthine. A single amino acid exchange, tyrosine 191 to leucine, is sufficient to convert E. coli PNP-II into an enzyme with the specificity of conventional trimeric PNPs, but the reciprocal mutation in human PNP, valine 195 to tyrosine, does not elicit xanthosine phosphorylase activity in the human enzyme.",
author = "Gert Dandanell and R.H. Szczepanowski and B. Kierdaszuk and D. Shugar and M. Bochtler",
note = "Keywords: PNP-II; xapA gene; biochemical characterization; crystal structure; phosphorolysis",
year = "2005",
doi = "10.1016/j.jmb.2005.02.019",
language = "English",
volume = "348",
pages = "113--25",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "1",

}

RIS

TY - JOUR

T1 - Escherichia coli Purine Nucleoside Phosphorylase II, the Product of the xapA Gene

AU - Dandanell, Gert

AU - Szczepanowski, R.H.

AU - Kierdaszuk, B.

AU - Shugar, D.

AU - Bochtler, M.

N1 - Keywords: PNP-II; xapA gene; biochemical characterization; crystal structure; phosphorolysis

PY - 2005

Y1 - 2005

N2 - Purine nucleoside phosphorylases (PNPs, E. C. 2.4.2.1) use orthophosphate to cleave the N-glycosidic bond of ß-(deoxy)ribonucleosides to yield a-(deoxy)ribose 1-phosphate and the free purine base. Escherichia coli PNP-II, the product of the xapA gene, is similar to trimeric PNPs in sequence, but has been reported to migrate as a hexamer and to accept xanthosine with comparable efficiency to guanosine and inosine, the usual physiological substrates for trimeric PNPs. Here, we present a detailed biochemical characterization and the crystal structure of E. coli PNP-II. In three different crystal forms, PNP-II trimers dimerize, leading to a subunit arrangement that is qualitatively different from the "trimer of dimers" arrangement of conventional high molecular mass PNPs. Crystal structures are compatible with similar binding modes for guanine and xanthine, with a preference for the neutral over the monoanionic form of xanthine. A single amino acid exchange, tyrosine 191 to leucine, is sufficient to convert E. coli PNP-II into an enzyme with the specificity of conventional trimeric PNPs, but the reciprocal mutation in human PNP, valine 195 to tyrosine, does not elicit xanthosine phosphorylase activity in the human enzyme.

AB - Purine nucleoside phosphorylases (PNPs, E. C. 2.4.2.1) use orthophosphate to cleave the N-glycosidic bond of ß-(deoxy)ribonucleosides to yield a-(deoxy)ribose 1-phosphate and the free purine base. Escherichia coli PNP-II, the product of the xapA gene, is similar to trimeric PNPs in sequence, but has been reported to migrate as a hexamer and to accept xanthosine with comparable efficiency to guanosine and inosine, the usual physiological substrates for trimeric PNPs. Here, we present a detailed biochemical characterization and the crystal structure of E. coli PNP-II. In three different crystal forms, PNP-II trimers dimerize, leading to a subunit arrangement that is qualitatively different from the "trimer of dimers" arrangement of conventional high molecular mass PNPs. Crystal structures are compatible with similar binding modes for guanine and xanthine, with a preference for the neutral over the monoanionic form of xanthine. A single amino acid exchange, tyrosine 191 to leucine, is sufficient to convert E. coli PNP-II into an enzyme with the specificity of conventional trimeric PNPs, but the reciprocal mutation in human PNP, valine 195 to tyrosine, does not elicit xanthosine phosphorylase activity in the human enzyme.

U2 - 10.1016/j.jmb.2005.02.019

DO - 10.1016/j.jmb.2005.02.019

M3 - Journal article

VL - 348

SP - 113

EP - 125

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 1

ER -

ID: 94781