4.1.2.50	748175	 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	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24990950&form=6&db=m	
4.1.2.50	717029	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	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18259064&form=6&db=m	
4.1.2.50	702280	Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase	Biochemistry	48	2301-2303	2009	Escherichia coli	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19231875&form=6&db=m	
4.1.2.50	726593	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	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24816091&form=6&db=m