Literature summary for 4.1.99.12 extracted from

Liao, D.I.; Zheng, Y.J.; Viitanen, P.V.; Jordan, D.B.
Structural definition of the active site and catalytic mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase (2002), Biochemistry, 41, 1795-1806.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pyricularia grisea

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, crystallization of different enzyme complexes: E-SO42-, E-SO42-Mg2+, E-SO42-Mn2+, E-SO42-Mn2+-glycerol, and E-SO42-Zn2+ complexes with X-ray diffraction structure determination and and analysis at resolutions that extend to 1.55 A, 0.98 A, 1.60 A, 1.16 A, and 1.00 A, respectively, divalent cation-free enzyme from 24-30% PEG 5000 monomethyl ether, 0.2 M Li2SO4, and 0.1 M MES-NaOH, pH 6.0-6.5, by the hanging drop vapor diffusion method, to prepare divalent cation-containing crystals, 200 mM MgCl2, 200 mM MnCl2, or 200 mM zinc acetate are added to the crystals for 8-16 h in soaking solutions of the well solutions omitting Li2SO4 and 4% higher in the concentration of PEG 5000 monomethyl ether	Pyricularia grisea

Crystallization (Comment)

Organism

purified recombinant enzyme, crystallization of different enzyme complexes: E-SO42-, E-SO42-Mg2+, E-SO42-Mn2+, E-SO42-Mn2+-glycerol, and E-SO42-Zn2+ complexes with X-ray diffraction structure determination and and analysis at resolutions that extend to 1.55 A, 0.98 A, 1.60 A, 1.16 A, and 1.00 A, respectively, divalent cation-free enzyme from 24-30% PEG 5000 monomethyl ether, 0.2 M Li2SO4, and 0.1 M MES-NaOH, pH 6.0-6.5, by the hanging drop vapor diffusion method, to prepare divalent cation-containing crystals, 200 mM MgCl2, 200 mM MnCl2, or 200 mM zinc acetate are added to the crystals for 8-16 h in soaking solutions of the well solutions omitting Li2SO4 and 4% higher in the concentration of PEG 5000 monomethyl ether

Pyricularia grisea

Metals/Ions

Metals/Ions	Comment	Organism
Mg2+	required, two Mg2+ cations that bind to the oxygen substituents of the C2, C3, C4, and phosphate groups of the substrate, the side chains of Glu37 and His153, and water molecules	Pyricularia grisea
Mn2+	binding structure, overview	Pyricularia grisea
additional information	the position of the metal cofactors and the substrates phosphate group are further stabilized by an extensive hydrogen-bond and salt-bridge network, overview	Pyricularia grisea
sulfate	binding structure at the active site, overview	Pyricularia grisea
Zn2+	binding structure, overview	Pyricularia grisea

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-ribulose 5-phosphate	Pyricularia grisea	-	formate + L-3,4-dihydroxy-2-butanone-4-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Pyricularia grisea	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate	active site structure and catalytic mechanism, modeling of the substrate ribulose 5-phosphate bound in the active site with the phosphate group anchored at the sulfate site and the placement of the ribulose group guided by the glycerol site, the catalytic reaction involves residues Asp41, Cys66, and Glu174, and the Asp99-His136 dyad	Pyricularia grisea	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-ribulose 5-phosphate	-	Pyricularia grisea	formate + L-3,4-dihydroxy-2-butanone-4-phosphate	-	?
additional information	the position of the metal cofactors and the substrates phosphate group are further stabilized by an extensive hydrogen-bond and salt-bridge network, overview	Pyricularia grisea	?	-	?

Subunits

Subunits	Comment	Organism
dimer	determination of the active sites in the homodimer, crystal structure, overview	Pyricularia grisea