On the origin of deoxypentoses: Evidence to support a glucose progenitor in the biosynthesis of calicheamicin

Tsion Bililign; Erica M. Shepard; Joachim Ahlert; Jon S. Thorson

doi:10.1002/1439-7633(20021104)3:11<1143::AID-CBIC1143>3.0.CO;2-W

On the origin of deoxypentoses: Evidence to support a glucose progenitor in the biosynthesis of calicheamicin

Tsion Bililign, Erica M. Shepard, Joachim Ahlert, Jon S. Thorson

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

17 Scopus citations

Abstract

Sweet by nature: While the biosyntheses of deoxyhexoses and deoxyribose are well characterized, the biosynthesis of the unique deoxypentose ligands of many natural products is lacking. Our characterization of an enzyme involved in calicheamicin (1) biosynthesis (CalS8, an NDP-α-D-glucose dehydrogenase or GlcDH) suggests a general model in which GlcDHs commit sugar nucleotides to the biosynthesis of secondary metabolite deoxypentose ligands.

Original language	English
Pages (from-to)	1143-1146
Number of pages	4
Journal	ChemBioChem
Volume	3
Issue number	11
DOIs	https://doi.org/10.1002/1439-7633(20021104)3:11<1143::AID-CBIC1143>3.0.CO;2-W
State	Published - Nov 4 2002

Keywords

Carbohydrates
Deoxysugars
Enzymes
Metabolism
Natural products

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Organic Chemistry

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10.1002/1439-7633(20021104)3:11<1143::AID-CBIC1143>3.0.CO;2-W

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abstract = "Sweet by nature: While the biosyntheses of deoxyhexoses and deoxyribose are well characterized, the biosynthesis of the unique deoxypentose ligands of many natural products is lacking. Our characterization of an enzyme involved in calicheamicin (1) biosynthesis (CalS8, an NDP-α-D-glucose dehydrogenase or GlcDH) suggests a general model in which GlcDHs commit sugar nucleotides to the biosynthesis of secondary metabolite deoxypentose ligands.",

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AU - Bililign, Tsion

AU - Shepard, Erica M.

AU - Ahlert, Joachim

AU - Thorson, Jon S.

PY - 2002/11/4

Y1 - 2002/11/4

N2 - Sweet by nature: While the biosyntheses of deoxyhexoses and deoxyribose are well characterized, the biosynthesis of the unique deoxypentose ligands of many natural products is lacking. Our characterization of an enzyme involved in calicheamicin (1) biosynthesis (CalS8, an NDP-α-D-glucose dehydrogenase or GlcDH) suggests a general model in which GlcDHs commit sugar nucleotides to the biosynthesis of secondary metabolite deoxypentose ligands.

AB - Sweet by nature: While the biosyntheses of deoxyhexoses and deoxyribose are well characterized, the biosynthesis of the unique deoxypentose ligands of many natural products is lacking. Our characterization of an enzyme involved in calicheamicin (1) biosynthesis (CalS8, an NDP-α-D-glucose dehydrogenase or GlcDH) suggests a general model in which GlcDHs commit sugar nucleotides to the biosynthesis of secondary metabolite deoxypentose ligands.

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KW - Deoxysugars

KW - Enzymes

KW - Metabolism

KW - Natural products

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On the origin of deoxypentoses: Evidence to support a glucose progenitor in the biosynthesis of calicheamicin

Abstract

Keywords

ASJC Scopus subject areas

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