The Crystal Structure of N 10 -Formyltetrahydrofolate Synthetase from Moorella thermoacetica †,‡
✍ Scribed by Radfar, Ramin; Shin, Ronald; Sheldrick, George M.; Minor, Wladek; Lovell, Charles R.; Odom, Jerome D.; Dunlap, R. Bruce; Lebioda, Lukasz
- Book ID
- 126209598
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 784 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0006-2960
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## Abstract Sau3 A and Hind III restriction fragments of __Clostridium cylindrosporum__ genomic DNA were used to isolate clones containing 80% of the __N__^10^‐H~4~folate synthetase gene in a 5′ fragment and the remaining 20% of the gene in the 3′ fragment. These fragments were joined at a common S
The monofunctional enzyme 10-formyltetrahydrofolate synthetase (THFS), which is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways, has been subcloned, purified, and crystallized. The crystals belong to space group P2