Formyltetrahydrofolate synthetase-catalyzed formation of ATP from carbamyl phosphate and ADP. Evidence for a formyl phosphate intermediate in the enzyme's catalytic mechanism.
Open Access
- 1 July 1976
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 251 (13) , 4159-4161
- https://doi.org/10.1016/s0021-9258(17)33370-7
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Electron paramagnetic resonance and water proton relaxation rate studies of formyltetrahydrofolate synthetase-manganous ion complexes. Evidence for involvement of substrates in the promotion of a catalytically competent active site.Journal of Biological Chemistry, 1975
- Equilibrium and water proton relaxation rate enhancement properties of formyltetrahydrofolate synthetase-manganous ion-substrate complexes.Journal of Biological Chemistry, 1975
- Formyltetrahydrofolate SynthetasePublished by Elsevier ,1972
- On the Possible Involvement of a Carbonyl Phosphate Intermediate in the Adenosine Triphosphate-dependent Carboxylation of BiotinJournal of Biological Chemistry, 1972
- Evidence against the Folate-mediated Formylation of Formyl-accepting Methionyl Transfer Ribonucleic Acid in Streptococcus faecalis RJournal of Biological Chemistry, 1970
- Formate MetabolismPublished by Elsevier ,1963
- Formyltetrahydrofolate SynthetasePublished by Elsevier ,1962
- Formyltetrahydrofolate SynthetasePublished by Elsevier ,1962
- FORMYLTETRAHYDROFOLATE SYNTHETASE .3. STUDIES ON MECHANISM OF REACTION1962
- FORMYLTETRAHYDROFOLATE SYNTHETASE .1. ISOLATION AND CRYSTALLIZATION OF ENZYME1962