Enzymes
| UniProtKB help_outline | 3 proteins |
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- 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 21 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- 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 H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (6S)-5,6,7,8-tetrahydrofolate Identifier CHEBI:57453 (Beilstein: 10223255) help_outline Charge -2 Formula C19H21N7O6 InChIKeyhelp_outline MSTNYGQPCMXVAQ-RYUDHWBXSA-L SMILEShelp_outline Nc1nc2NC[C@H](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 40 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5-hydroxymethyl-dUMP Identifier CHEBI:90409 Charge -2 Formula C10H13N2O9P InChIKeyhelp_outline WEBVWKFGRVLCNS-XLPZGREQSA-L SMILEShelp_outline N1([C@@H]2O[C@H](COP([O-])([O-])=O)[C@H](C2)O)C(NC(=O)C(=C1)CO)=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:48424 | RHEA:48425 | RHEA:48426 | RHEA:48427 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Cloning, expression, purification, and characterization of 2'-deoxyuridylate hydroxymethylase from phage SPO1.
Schellenberger U., Livi L.L., Santi D.V.
2'-Deoxyuridylate hydroxymethylase (dUMP-hmase) from phage SPO1 has been cloned and expressed in Escherichia coli. In crude extracts, the enzyme represents about 25% of the soluble protein and has a higher specific activity than the most purified preparation yet reported. The enzyme was purified t ... >> More
2'-Deoxyuridylate hydroxymethylase (dUMP-hmase) from phage SPO1 has been cloned and expressed in Escherichia coli. In crude extracts, the enzyme represents about 25% of the soluble protein and has a higher specific activity than the most purified preparation yet reported. The enzyme was purified to homogeneity by ion-exchange and hydrophobic chromatography. The subunits of dUMP-hmase are 45 kDa by SDS-PAGE and form dimers with a molecular mass of 89.2 kDa by analytical centrifugation. In addition to the normal reaction, dUMP-hmase catalyzes the 5,10-methylene-5,6,7,8-tetrahydrofolate (CH2H4folate)-independent tritium exchange of [5-3H]dUMP for protons of water and dehalogenation of 5-bromo-2'-deoxy-uridine-5'-monophosphate; the enzyme also forms a covalent binary adduct with pyridoxal 5'-monophosphate and a covalent ternary complex with 5-fluoro-2'-deoxyuridine-5'-monophosphate and CH2H4folate. Folic acid inhibits the tritium release catalyzed by dUMP-hmase in the presence of cofactor but has no effect on the catalysis of cofactor-independent tritium exchange. << Less
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Deoxyuridylate-hydroxymethylase of bacteriophage SPO1.
Wilhelm K., Rueger W.
Phage SPO1 of Bacillus subtilis carries hydroxymethyl-deoxyuridylate in place of thymidylate in its DNA. The enzyme, responsible for the conversion of dUMP to HmdUMP, is a dUMP hydroxymethylase, encoded by the SPO1 gene 29. Here we describe the cloning and sequencing of the gene and the overexpres ... >> More
Phage SPO1 of Bacillus subtilis carries hydroxymethyl-deoxyuridylate in place of thymidylate in its DNA. The enzyme, responsible for the conversion of dUMP to HmdUMP, is a dUMP hydroxymethylase, encoded by the SPO1 gene 29. Here we describe the cloning and sequencing of the gene and the overexpression of the gene product. DNA hybridization using the DNA of bacteriophage T4 dCMP-hydroxymethylase gene as a probe, allowed us to identify and map g29 on a 3.9-kb restriction fragment, EcoRI*11. We determined the nucleotide sequence. One of the open reading frames detected, coding for a putative 44.6-kDa protein, showed significant amino acid homologies with all known thymidylate synthases. Gp29 was overexpressed in the pT7 system. Extracts prepared from induced cells show hydroxymethylase activity in a tritium release assay. << Less