Formyltetrahydrofolate synthetase-catalyzed formation of ATP from carbamyl phosphate and ADP. Evidence for a formyl phosphate intermediate in the enzyme's catalytic mechanism.-Reference-Cited by-同舟云学术

Formyltetrahydrofolate synthetase-catalyzed formation of ATP from carbamyl phosphate and ADP. Evidence for a formyl phosphate intermediate in the enzyme's catalytic mechanism.

Published:1976-07 Issue:13 Volume:251 Page:4159-4161
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Buttlaire D H,Himes R H,Reed G H

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference11 articles.

1. Formyltetrahydrofolate Synthetas

2. Equilibrium and water proton relaxation rate enhancement properties of formyltetrahydrofolate synthetase-manganous ion-substrate complexes.

3. 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.

4. On the Possible Involvement of a Carbonyl Phosphate Intermediate in the Adenosine Triphosphate-dependent Carboxylation of Biotin

5. Rat Liver Glutamine Synthetase

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