Enzymes activity association with carbon metabolism

The tetrahydrofolates do not function as tightly enzyme-bound coenzymes. Rather, they function as cosubstrates for a variety of enzymes associated with one-carbon metabolism. /Vl0-formyltetrahydrofolate is produced enzymatically from tetrahydrofolate and formate in an ATP-linked process in which formate is activated by phosphorylation to formyl phosphate the formyl group of formyl phosphate is then transferred to A10 of tetrahydrofolate. A10-Formyltetrahydrofolate is a formyl donor substrate for some enzymes and is interconvertible with A5,A10-methenyltetrahydrofolate by the action of cyclohydrolase. 

Vitamin K cycle—metabolic interconversions of vitamin K associated with the synthesis of vitamin K-dependent clotting factors. Vitamin K1 or K2 is activated by reduction to the hydroquinone form (KH2). Stepwise oxidation to vitamin K epoxide (KO) is coupled to prothrombin carboxylation by the enzyme carboxylase. The reactivation of vitamin K epoxide is the warfarin-sensitive step (warfarin). The R on the vitamin K molecule represents a 20-carbon phytyl side chain in vitamin Ki and a 30- to 65-carbon polyprenyl side chain in vitamin K2. 

McLean, P., Reid, E., and Gurney, M. W., Effect of azo-dye carcinogenesis on enzymes concerned with urea synthesis in the rat. Biochem. J. 91, 464-473 (1964). McLean, P., and Rossi, F., Changes in the activities of urea-cycle enzymes after the administration of carbon tetrachloride. Biochem. J. 91, 261-270 (1964). McMurray, W. C., Mohyuddin, F., Bayer, S. M., and Rathbun, J. C., Citrul-linuria a disorder of amino acid metabolism associated with mental retardation. Int. Copenhagen Congr. Sci. Study Meat. Retard., Proc. 3rd 1, 117 (1964). McMurray, W. C., Rathbun, J. C., Mohyuddin, F., and Koegler, S. J., Citrul-linuria. Pediatrics 32, 347-357 (1963). 

---