Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase.
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.
McCarty
Reid M
RM
Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, Arizona 85721, USA.
Somogyi
Arpád
A
Bandarian
Vahe
V
D019757:Carbon-Oxygen Lyases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019798:Neopterin / Q000031:analogs & derivatives / Q000378:metabolism; D011621:Pteridines / Q000378:metabolism*
D029968:Escherichia coli Proteins; D011621:Pteridines; C013490:dihydroneopterin triphosphate; C005063:2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine; D019798:Neopterin; D019757:Carbon-Oxygen Lyases; C548374:QueD protein, E coli