Enzymes
| UniProtKB help_outline | 28,186 proteins |
| Enzyme class help_outline |
|
| GO Molecular Function help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline dUMP Identifier CHEBI:246422 (Beilstein: 4011255) help_outline Charge -2 Formula C9H11N2O8P InChIKeyhelp_outline JSRLJPSBLDHEIO-SHYZEUOFSA-L SMILEShelp_outline O[C@H]1C[C@@H](O[C@@H]1COP([O-])([O-])=O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate Identifier CHEBI:15636 (Beilstein: 5468618) help_outline Charge -2 Formula C20H21N7O6 InChIKeyhelp_outline QYNUQALWYRSVHF-OLZOCXBDSA-L SMILEShelp_outline [H][C@]12CNc3nc(N)[nH]c(=O)c3N1CN(C2)c1ccc(cc1)C(=O)N[C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 22 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 7,8-dihydrofolate Identifier CHEBI:57451 Charge -2 Formula C19H19N7O6 InChIKeyhelp_outline OZRNSSUDZOLUSN-LBPRGKRZSA-L SMILEShelp_outline Nc1nc2NCC(CNc3ccc(cc3)C(=O)N[C@@H](CCC([O-])=O)C([O-])=O)=Nc2c(=O)[nH]1 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dTMP Identifier CHEBI:63528 (Beilstein: 3916216) help_outline Charge -2 Formula C10H13N2O8P InChIKeyhelp_outline GYOZYWVXFNDGLU-XLPZGREQSA-L SMILEShelp_outline Cc1cn([C@H]2C[C@H](O)[C@@H](COP([O-])([O-])=O)O2)c(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:12104 | RHEA:12105 | RHEA:12106 | RHEA:12107 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline | ||||
| EcoCyc help_outline | ||||
| M-CSA help_outline |
Publications
-
Purification of thymidylate synthetase from enzyme-poor sources by affinity chromatography.
Slavik K., Slavikova V.
-
Thymidylate synthetase purified to homogeneity from human leukemic cells.
Lockshin A., Moran R.G., Danenberg P.V.
Thymidylate synthetase (5,10-methylenetetrahydrofolate:dUMP C-methyltransferase, EC 2.1.1.45) from a human leukemic cell line has been purified to homogeneity with one-step affinity column chromatography. The purified enzyme has a specific activity of 3.8 micron/min per mg of protein, which corres ... >> More
Thymidylate synthetase (5,10-methylenetetrahydrofolate:dUMP C-methyltransferase, EC 2.1.1.45) from a human leukemic cell line has been purified to homogeneity with one-step affinity column chromatography. The purified enzyme has a specific activity of 3.8 micron/min per mg of protein, which corresponds to a turnover number of 250. These are the highest values reported for a thymidylate synthetase from neoplastic tissue. A ratio of 1.7 mol of 5-fluoro-2'-deoxyuridylate binds per mol of enzyme in the presence of 5,10-methylenetetrahydrofolate. The ternary complex so formed migrates intact on denaturing gels and can be precipitated with trichloroacetic acid; however, urea dissociates the ternary complex. The human thymidylate synthetase is composed of two subunits of 33,000 daltons each. It contains more residues of cysteine, glycine, and arginine and fewer of histidine than the well-studied thymidylate synthetase from Lactobacillus casei. << Less
Proc Natl Acad Sci U S A 76:750-754(1979) [PubMed] [EuropePMC]
-
The enzymatic synthesis of thymidylate. I. Early steps in the purification of thymidylate synthetase of Escherichia coli.
WAHBA A.J., FRIEDKIN M.