A 5,10-methylenetetrahydrofolate dehydrogenase: 5,10-methenyltetrahydrofolate cyclohydrolase protein from Pisum sativum

Purification, crystallization, and preli

Purification, crystallization, and preliminary X-ray studies of a bifunctional 5,10-methenyl/methylene tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli

✍ Edwin Cheung; Linda D'Ari; Jesse C. Rabinowitz; David H. Dyer; Jie-Yu Huang; Bar 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 32 KB 👁 2 views

A bifunctional enzyme that catalyzes the conversion of formyltetrahydrofolate to methylene-tetrahydrofolate (5,10methenyltetrahydrofolate cyclohydrolase and 5,10-methylene tetrahydrofolate dehydrogenase), has been subcloned from a cDNA library, purified to homogeneity, and crystallized. The crystals