EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
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 |
24990950 |
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 |
18259064 |
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 |
19231875 |
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 |
24816091 |