| Title | Date | PubMed ID |
|---|
| 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. | 2014 Aug 22 | 24990950 |
| Structural basis of a novel activity of bacterial 6-pyruvoyltetrahydropterin synthase homologues distinct from mammalian 6-pyruvoyltetrahydropterin synthase activity. | 2014 May | 24816091 |
| Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase. | 2009 Mar 24 | 19231875 |
| Crystallization and preliminary X-ray characterization of queD from Bacillus subtilis, an enzyme involved in queuosine biosynthesis. | 2008 Feb 1 | 18259064 |