Enzyme

Download
EC Tree
     2. Transferases
        2.8 Transferring sulfur-containing groups
            2.8.3 CoA-transferases
ID:2.8.3.16
Description:Formyl-CoA transferase.
Alternative Name: Formyl-coenzyme A transferase.
Formyl-CoA oxalate CoA-transferase.
Cath: 1.10.287.1620; 1.20.5.1530; 3.30.1540.10; 3.30.60.110; 3.40.50.10540; 3.40.50.12220;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.8.3.16
BRENDA Enzyme Link: BRENDA 2.8.3.16
KEGG Enzyme Link: KEGG2.8.3.16
BioCyc Enzyme Link: BioCyc 2.8.3.16
ExPASy Enzyme Link: ExPASy2.8.3.16
EC2PDB Enzyme Link: EC2PDB 2.8.3.16
ExplorEnz Enzyme Link: ExplorEnz 2.8.3.16
PRIAM enzyme-specific profiles Link: PRIAM 2.8.3.16
IntEnz Enzyme Link: IntEnz 2.8.3.16
MEDLINE Enzyme Link: MEDLINE 2.8.3.16
MSA:

2.8.3.16;

Phylogenetic Tree:

2.8.3.16;

Uniprot:
M-CSA:
RHEA:16545 formyl-CoA + oxalate = formate + oxalyl-CoA
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[C;H0;+0:4](=[*:5])-[*:6].[*:7]=[CH;+0:8]-[*:9]>>[*:7]=[C;H0;+0:8](-[*:9])-[C;H0;+0:4](=[*:5])-[*:6].[*:1]=[CH;+0:2]-[*:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase.Toyota CG, Berthold CL, Gruez A, Jónsson S, Lindqvist Y, Cambillau C, Richards NG2008 Apr18245280
The crystal structure of the Escherichia coli YfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases.Gruez A, Roig-Zamboni V, Valencia C, Campanacci V, Cambillau C2003 Sep 512844490