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Literature summary extracted from

  • Daniels, J.N.; Wuebbens, M.M.; Rajagopalan, K.V.; Schindelin, H.
    Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency (2008), Biochemistry, 47, 615-626.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

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

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 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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.12 Escherichia coli P30749
-
-
2.8.1.12 Staphylococcus aureus
-
-
-

Purification (Commentary)

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

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 catalytic mechanism, structure function-relationship, overview Staphylococcus aureus
a
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
a

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
-
 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
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.8.1.12 MPT synthase
-
 Staphylococcus aureus
2.8.1.12 MPT synthase
-
 Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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