EC Number | Cloned (Comment) | Organism |
---|---|---|
2.8.1.12 | genes moaE and moaD, expression of His6-tagged MoaE and MoaD in Escherichia coli strain Rosetta (DE3) | Staphylococcus aureus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.8.1.12 | purified recombinant apo form molybdopterin synthase and molybdopterin synthase-precursor Z complex using wild-type and mutant K126A MoeE, X-ray diffraction structure determination and analysis, structure modeling with the enzyme from Staphylococcu aureus, overview | Escherichia coli |
2.8.1.12 | purified recombinant His-tagged apo form molybdopterin synthase and molybdopterin synthase-precursor Z complex using wild-type and mutant K123A MoeE, 10 mg/ml protein in a buffer containing 50 mM Tris-HCl, pH 8.0, and 50 mM NaCl, mixed with a precipitant consisting of 2.0 M sodium formate and 0.1 M sodium acetate, pH 5.3, at 22°C, 2 days, for the enzyme complex with precursor Z, 18% w/v PEG 8000, 0.1% polyvinylpyrrollidone K15, and 0.1 M Tris-HCl, pH 8.0, at 4°C is used, X-ray diffraction structure determination and analysis at 2.0 A resolution for the apoenzyme and at 2.5 A resolution for the enzyme complex, molecular replacement with MOLREP, modeling using the cyrstal structure of the Escherichia coli MPT synthase, overview | Staphylococcus aureus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.8.1.12 | E125K | inactive mutant | Staphylococcus aureus |
2.8.1.12 | E128K | inactive mutant | Escherichia coli |
2.8.1.12 | K123A | site-directed mutagenesis, mutant of MoaE | Staphylococcus aureus |
2.8.1.12 | K126A | site-directed mutagenesis, mutant of MoaE | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.8.1.12 | cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O | Staphylococcus aureus | - |
molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | - |
? | |
2.8.1.12 | cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O | Escherichia coli | - |
molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.8.1.12 | Escherichia coli | P30749 | - |
- |
2.8.1.12 | Staphylococcus aureus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.8.1.12 | recombinant His6-tagged MoaE and MoaD from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration | Staphylococcus aureus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.8.1.12 | cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O = molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | catalytic mechanism, structure function-relationship, overview | Staphylococcus aureus | |
2.8.1.12 | cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O = molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | catalytic mechanism, structure function-relationship, overview | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.8.1.12 | cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O | - |
Staphylococcus aureus | molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | - |
? | |
2.8.1.12 | cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O | - |
Escherichia coli | molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | - |
? | |
2.8.1.12 | cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O | via reaction intermediate, overview | Staphylococcus aureus | molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | - |
? | |
2.8.1.12 | cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + H2O | via reaction intermediate, overview | Escherichia coli | molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.8.1.12 | heterotetramer | the MPT synthase protein consists of two large (MoaE) and two small (MoaD) subunits with the MoaD subunits located at opposite ends of a central MoaE dimer | Staphylococcus aureus |
2.8.1.12 | heterotetramer | the MPT synthase protein consists of two large (MoaE) and two small (MoaD) subunits with the MoaD subunits located at opposite ends of a central MoaE dimer | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.8.1.12 | MPT synthase | - |
Staphylococcus aureus |
2.8.1.12 | MPT synthase | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.8.1.12 | 22 | - |
assay at room temperature | Staphylococcus aureus |
2.8.1.12 | 22 | - |
assay at room temperature | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.8.1.12 | 7.2 | - |
assay at | Staphylococcus aureus |
2.8.1.12 | 7.2 | - |
assay at | Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.8.1.12 | metabolism | MPT synthase catalyzes the second step of molybdenum cafactor biosynthesis | Staphylococcus aureus |
2.8.1.12 | metabolism | MPT synthase catalyzes the second step of molybdenum cafactor biosynthesis | Escherichia coli |
2.8.1.12 | additional information | active site struture and substrate-binding and catalytically important residues, overview | Escherichia coli |
2.8.1.12 | additional information | active site struture and substrate-binding and catalytically important residues, overview. Interaction between Glu125 and precursor Z in the enzyme-precursor Z cocrystals | Staphylococcus aureus |
2.8.1.12 | physiological function | conversion of the sulfur- and metal-free precursor Z to mylobdopterin by MPT synthase involving the transfer of sulfur atoms from a C-terminal MoaD thiocarboxylate to the C-1' and C-2' positions of precursor Z. In the complex, precursor Z is bound by strictly conserved residues in a pocket at the MoaE dimer interface in close proximity of the C-terminal glycine of MoaD, conformational changes in a loop that participates in interactions with precursor Z | Staphylococcus aureus |
2.8.1.12 | physiological function | conversion of the sulfur- and metal-free precursor Z to mylobdopterin by MPT synthase involving the transfer of sulfur atoms from a C-terminal MoaD thiocarboxylate to the C-1' and C-2' positions of precursor Z. In the complex, precursor Z is bound by strictly conserved residues in a pocket at the MoaE dimer interface in close proximity of the C-terminal glycine of MoaD, conformational changes in a loop that participates in interactions with precursor Z | Escherichia coli |