Literature summary for 6.3.4.3 extracted from

D�Ari, L.; Cheung, E.; Rabinowitz, J.C.; Bolduc, J.M.; Huang, J.Y.; Stoddard, B.L.
Purification, crystallization, and preliminary X-ray studies of 10-formyltetrahydrofolate synthetase from Clostridia acidi-urici (1997), Proteins Struct. Funct. Genet., 27, 319-321.

Search for more literature for 6.3.4.3

Cloned(Commentary)

Cloned (Comment)	Organism
-	Clostridium acidi-urici

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Clostridium acidi-urici

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + formate + tetrahydrofolate	Clostridium acidi-urici	the enzyme is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Clostridium acidi-urici	-	monofunctional enzyme	-

Purification (Commentary)

Purification (Comment)	Organism
-	Clostridium acidi-urici

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + formate + tetrahydrofolate	-	Clostridium acidi-urici	ADP + phosphate + 10-formyltetrahydrofolate	-	?
ATP + formate + tetrahydrofolate	the enzyme is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways	Clostridium acidi-urici	?	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)