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Literature summary extracted from
- Thiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins (2001), J. Biol. Chem., 276, 36268-36274.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 2.8.1.12 | genes moaD and moaE,expression of His-tagged wild-type and mutant protein in Escherichia coli strain M15 | Escherichia coli |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 2.8.1.12 | 6900 | - |
2 * 6900, MoaD, + 2 * 16500, MoaE, SDS-PAGE, composed of two small MoaD and two large subunits MoaE. Both forms of MoaD, carboxylated and thiocarboxylated, are monomeric and are able to form a heterotetrameric complex after coincubation in equimolar ratios with MoaE, but only the thiocarboxylated MPT synthase complex is able to convert precursor Z in vitro to MPT | Escherichia coli |
| 2.8.1.12 | 16500 | - |
2 * 6900, MoaD, + 2 * 16500, MoaE, SDS-PAGE, composed of two small MoaD and two large subunits MoaE. Both forms of MoaD, carboxylated and thiocarboxylated, are monomeric and are able to form a heterotetrameric complex after coincubation in equimolar ratios with MoaE, but only the thiocarboxylated MPT synthase complex is able to convert precursor Z in vitro to MPT | Escherichia coli |
| 2.8.1.12 | 46100 | - |
carboxylated MPT synthase, gel filtration | Escherichia coli |
| 2.8.1.12 | 52800 | - |
thiocarboxylated MPT synthase, gel filtration | Escherichia coli |
Natural Substrates/ Products (Substrates)
| 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 | Escherichia coli | - |
molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.8.1.12 | Escherichia coli | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 2.8.1.12 | recombinant His-tagged wild-type and mutant protein from Escherichia coli strain M15 by nickel affinity chromatography and gel filtration. Elution of carboxylated or thiocarboxylated protein is induced by using a cleavage buffer containing 20 mM Tris/HCl, 500 mM NaCl, 0.1 mM EDTA, pH 8.0, with either 30 mM dithiothreitol or 30 mM ammonium sulfide, respectively. The cleavage reaction is performed at 4°C for at least 24 h | Escherichia coli |
Reaction
| 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 | two-step reaction of MPT synthesis where the dithiolene is generated by two thiocarboxylates derived from a single tetrameric MPT synthase, hypothetical model for the conversion of precursor Z to molybdopterin in the MPT synthase reaction, overview | Escherichia coli |
Substrates and Products (Substrate)
| 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 | - |
Escherichia coli | molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein | - |
? | |
| 2.8.1.12 | additional information | in vitro generation of carboxylated and thiocarboxylated MoaD, overview | Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 2.8.1.12 | ? | x * 8757.94, recombinant carboxylated MoaD, sequence calculation, x * 8774.03, recombinant thiocarboxylated MoaD, sequence calculation, x * 8757.72, recombinant carboxylated MoaD, mass spectrometry, x * 8774.00, recombinant thiocarboxylated MoaD, mass spectrometry | Escherichia coli |
| 2.8.1.12 | heterotetramer | 2 * 6900, MoaD, + 2 * 16500, MoaE, SDS-PAGE, composed of two small MoaD and two large subunits MoaE. Both forms of MoaD, carboxylated and thiocarboxylated, are monomeric and are able to form a heterotetrameric complex after coincubation in equimolar ratios with MoaE, but only the thiocarboxylated MPT synthase complex is able to convert precursor Z in vitro to MPT | Escherichia coli |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 2.8.1.12 | additional information | Both forms of MoaD, carboxylated and thiocarboxylated, are monomeric and are able to form a heterotetrameric complex after coincubation in equimolar ratios with MoaE, but only the thiocarboxylated MPT synthase complex is able to convert precursor Z in vitro to MPT | Escherichia coli |
| 2.8.1.12 | physiological function | MPT is formed by incorporation of two sulfur atoms into precursor Z, which is catalyzed by MPT synthase. The thiocarboxylation of the C-terminus of MoaD serves as the source of sulfur that is transferred to precursor Z | Escherichia coli |
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