Abstract
To elucidate the early steps required during biosynthesis of a broad class of 7-deazapurine-containing natural products, we have studied the reaction catalyzed by Escherichia coli QueD, a 6-pyruvoyl-5,6,7,8-tetrahydropterin synthase (PTPS) homologue possibly involved in queuosine biosynthesis. While mammalian PTPS homologues convert 7,8-dihydroneopterin triphosphate (H(2)NTP) to 6-pyruvoyltetrahydropterin (PPH(4)) in biopterin biosynthesis, E. coli QueD catalyzes the conversion of H(2)NTP to 6-carboxy-5,6,7,8-tetrahydropterin (CPH(4)). E. coli QueD can also convert PPH(4) and sepiapterin to CPH(4), allowing a mechanism to be proposed.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Carbon-Oxygen Lyases / chemistry
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Carbon-Oxygen Lyases / genetics
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Carbon-Oxygen Lyases / metabolism*
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Escherichia coli / chemistry
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Neopterin / analogs & derivatives
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Neopterin / metabolism
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Pteridines / metabolism*
Substances
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Escherichia coli Proteins
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Pteridines
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dihydroneopterin triphosphate
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2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine
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Neopterin
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Carbon-Oxygen Lyases
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QueD protein, E coli