Enzymes
| UniProtKB help_outline | 3 proteins |
| Enzyme class help_outline |
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- Name help_outline 4-aminobenzoate Identifier CHEBI:17836 (Beilstein: 3904778; CAS: 2906-28-7) help_outline Charge -1 Formula C7H6NO2 InChIKeyhelp_outline ALYNCZNDIQEVRV-UHFFFAOYSA-M SMILEShelp_outline Nc1ccc(cc1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5-phospho-α-D-ribose 1-diphosphate Identifier CHEBI:58017 Charge -5 Formula C5H8O14P3 InChIKeyhelp_outline PQGCEDQWHSBAJP-TXICZTDVSA-I SMILEShelp_outline O[C@H]1[C@@H](O)[C@H](O[C@@H]1COP([O-])([O-])=O)OP([O-])(=O)OP([O-])([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 H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate Identifier CHEBI:72778 Charge -2 Formula C11H14NO7P InChIKeyhelp_outline UKBUHWIOGWAJEO-DBIOUOCHSA-L SMILEShelp_outline Nc1ccc(cc1)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (Beilstein: 1900390; CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 997 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:35815 | RHEA:35816 | RHEA:35817 | RHEA:35818 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Purification, kinetic characterization, and site-directed mutagenesis of Methanothermobacter thermautotrophicus RFAP Synthase Produced in Escherichia coli.
Bechard M.E., Farahani P., Greene D., Pham A., Orry A., Rasche M.E.
Methane-producing archaea are among a select group of microorganisms that utilize tetrahydromethanopterin (H<sub>4</sub>MPT) as a one-carbon carrier instead of tetrahydrofolate. In H<sub>4</sub>MPT biosynthesis, β-ribofuranosylaminobenzene 5'-phosphate (RFAP) synthase catalyzes the production of R ... >> More
Methane-producing archaea are among a select group of microorganisms that utilize tetrahydromethanopterin (H<sub>4</sub>MPT) as a one-carbon carrier instead of tetrahydrofolate. In H<sub>4</sub>MPT biosynthesis, β-ribofuranosylaminobenzene 5'-phosphate (RFAP) synthase catalyzes the production of RFAP, CO<sub>2</sub>, and pyrophosphate from <i>p</i>-aminobenzoic acid (<i>p</i>ABA) and phosphoribosyl-pyrophosphate (PRPP). In this work, to gain insight into amino acid residues required for substrate binding, RFAP synthase from <i>Methanothermobacter thermautotrophicus</i> was produced in <i>Escherichia coli</i>, and site-directed mutagenesis was used to alter arginine 26 (R26) and aspartic acid 19 (D19), located in a conserved sequence of amino acids resembling the <i>p</i>ABA binding site of dihydropteroate synthase. Replacement of R26 with lysine increased the <i>K<sub>M</sub></i> for <i>p</i>ABA by an order of magnitude relative to wild-type enzyme without substantially altering the <i>K<sub>M</sub></i> for PRPP. Although replacement of D19 with alanine produced inactive enzyme, asparagine substitution allowed retention of some activity, and the <i>K</i> <sub>M</sub> for <i>p</i>ABA increased about threefold relative to wild-type enzyme. A molecular model developed by threading RFAP synthase onto the crystal structure of homoserine kinase places R26 in the proposed active site. In the static model, D19 is located close to the active site, yet appears too far away to influence ligand binding directly. This may be indicative of the protein conformational change predicted previously in the Bi-Ter kinetic mechanism and/or formation of the active site at the interface of two subunits. Due to the vital role of RFAP synthase in H<sub>4</sub>MPT biosynthesis, insights into the mode of substrate binding and mechanism could be beneficial for developing RFAP synthase inhibitors designed to reduce the production of methane as a greenhouse gas. << Less