Enzyme

Download
EC Tree
     6. Ligases
        6.3 Forming carbon-nitrogen bonds
            6.3.4 Other carbon-nitrogen ligases
ID:6.3.4.3
Description:Formate--tetrahydrofolate ligase.
Alternative Name: Tetrahydrofolic formylase.
Tetrahydrofolate formylase.
Formyltetrahydrofolate synthetase.
Prosite: PDOC00595;
PDB:
PDBScop
3DO6 8078440; 8078441; 8078440; 8078441;
3QUS 8017964; 8017965; 8017964; 8017965;
1FPM 8017964; 8017965; 8017964; 8017965;
1FP7 8017964; 8017965; 8017964; 8017965;
1EG7 8017964; 8017965; 8017964; 8017965;
 » show all

Cath: 1.10.8.770; 3.30.1510.10; 3.40.50.720; 3.40.50.10860; 3.40.50.300; 3.10.410.10;

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 6.3.4.3
BRENDA Enzyme Link: BRENDA 6.3.4.3
KEGG Enzyme Link: KEGG6.3.4.3
BioCyc Enzyme Link: BioCyc 6.3.4.3
ExPASy Enzyme Link: ExPASy6.3.4.3
EC2PDB Enzyme Link: EC2PDB 6.3.4.3
ExplorEnz Enzyme Link: ExplorEnz 6.3.4.3
PRIAM enzyme-specific profiles Link: PRIAM 6.3.4.3
IntEnz Enzyme Link: IntEnz 6.3.4.3
MEDLINE Enzyme Link: MEDLINE 6.3.4.3
MSA:

6.3.4.3;

Phylogenetic Tree:

6.3.4.3;

Uniprot:
M-CSA:
RHEA:20221 (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
RULE(radius=1) [*:1]-[NH;+0:2]-[*:3].[*:4]=[CH;+0:5]-[OH;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:1]-[N;H0;+0:2](-[*:3])-[CH;+0:5]=[*:4].[*:12]-[OH;+0:11].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Formyltetrahydrofolate synthetase. I. Isolation and crystallization of the enzyme.RABINOWITZ JC, PRICER WE Jr1962 Sep14489619
[Research on monocarbon compounds. I. The tetrahydrofolate formylase from pigeon liver. Purification and mechanism].JAENICKE L, BRODE E196113789141
Purification and properties of the formate-activating enzyme from Micrococcus aerogenes.WHITELEY HR, OSBORN MJ, HUENNEKENS FM1959 Jun13654413