Literature summary for 2.8.1.12 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

Organism	UniProt	Comment	Textmining
Escherichia coli	P30749	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant fully activated MoaD, MoaE, and the E141DELTA variant of MoaE	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

General Information	Comment	Organism
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