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Results 1 - 4 of 4
EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 4.1.2.50Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.50748175 Biochemical and structural studies of 6-carboxy-5,6,7,8-tetrahydropterin synthase reveal the molecular basis of catalytic promiscuity within the tunnel-fold superfamily J. Biol. Chem. 289 23641-23652 2014 Escherichia coli 24990950
Show all pathways known for 4.1.2.50Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.50717029 Crystallization and preliminary X-ray characterization of queD from Bacillus subtilis, an enzyme involved in queuosine biosynthesis Acta Crystallogr. Sect. F 64 119-122 2008 Bacillus subtilis 18259064
Show all pathways known for 4.1.2.50Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.50702280 Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase Biochemistry 48 2301-2303 2009 Escherichia coli 19231875
Show all pathways known for 4.1.2.50Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.50726593 Structural basis of a novel activity of bacterial 6-pyruvoyltetrahydropterin synthase homologues distinct from mammalian 6-pyruvoyltetrahydropterin synthase activity Acta Crystallogr. Sect. D 70 1212-1223 2014 Escherichia coli 24816091
Results 1 - 4 of 4