Literature summary for 2.8.3.16 extracted from

Jonsson, S.; Ricagno, S.; Lindqvist, Y.; Richards, N.G.
Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes (2004), J. Biol. Chem., 279, 36003-36012.

Search for more literature for 2.8.3.16

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization and structure determination of the enzyme/oxalyl-CoA complex, hanging drop technique. Crystallization and structure determination of the D169A, D169E, and D169S mutants	Oxalobacter formigenes

Protein Variants

Protein Variants	Comment	Organism
D169A	mutant enzyme is correctly folded and forms interlocked dimers, 1300fold decrease in activity	Oxalobacter formigenes
D169E	mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme	Oxalobacter formigenes
D169S	mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme	Oxalobacter formigenes

Inhibitors

Inhibitors	Comment	Organism	Structure
formate	-	Oxalobacter formigenes
oxalyl-CoA	-	Oxalobacter formigenes

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
81000	-	gel filtration	Oxalobacter formigenes

Organism

Organism	UniProt	Comment	Textmining
Oxalobacter formigenes	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
enzyme recombinantly expressed in Escherichia coli	Oxalobacter formigenes

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
formyl-CoA + oxalate	involvement of the Asp169 side chain in mediating enzyme-catalyzed CoA transfer via a series of anhydride intermediates	Oxalobacter formigenes	formate + oxalyl-CoA	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Oxalobacter formigenes

Synonyms

Synonyms	Comment	Organism
FRC	-	Oxalobacter formigenes

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
4.3	-	oxalate	-	Oxalobacter formigenes
4.3	-	formyl-CoA	-	Oxalobacter formigenes

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	additional information	Kis for formate is 17 mM, Kii for formate is 380 mM, Kis for oxalyl-CoA is 0.15 mM, Kii for oxalyl-CoA is 0.28 mM	Oxalobacter formigenes

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)