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Literature summary extracted from

  • Rudolph, M.J.; Wuebbens, M.M.; Turque, O.; Rajagopalan, K.V.; Schindelin, H.
    Structural studies of molybdopterin synthase provide insights into its catalytic mechanism (2003), J. Biol. Chem., 278, 14514-14522.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.1.12 purified recombinant MoaE, MoaD, and mutant MoeE E141DELTA, the MoaD-MoeB complex is crystallized using 1.1 M (NH4)2SO4 and 0.1 M HEPES, pH 7.5, as precipitant at a protein concentration of 15 mg/ml within 4-8 months, MoeE mutant E141DELTA at a protein concentration of 20 mg/ml is crystallized from a solution containing 600 mM sodium formate, 15% polyethylene glycol 4000, 10% isopropyl alcohol, and 100 mM Tris, pH 7.5, within 2-3 days, X-ray diffraction structure determination and analysis at 1.9-2.4 A resolution Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.8.1.12 E141DELTA site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, formate binding site structure in the E141DELTA MoaE variant, overview 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 P30749
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.1.12 recombinant fully activated MoaD, MoaE, and the E141DELTA variant of MoaE 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 catalytic mechanism, structure-function relationshipp analysis, 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
-
 Escherichia coli molybdopterin + 2 molybdopterin-synthase sulfur-carrier protein
-
 ?

General Information

EC Number General Information Comment Organism
2.8.1.12 additional information molybdopterin synthase contains a binding pocket for the terminal phosphate of molybdopterin, structure of the MoaD thiocarboxylate, overview. The MoaE homodimer shows conformational changes accompanying binding of the MoaD subunit, overview. Position of the thiocarboxylate sulfur at the C-terminus of MoaD Escherichia coli