EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.99.12 | expression in Escherichia coli | Pyricularia grisea |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.1.99.12 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.99.12 | 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 | |
4.1.99.12 | Mn2+ | binding structure, overview | Pyricularia grisea | |
4.1.99.12 | 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 | |
4.1.99.12 | sulfate | binding structure at the active site, overview | Pyricularia grisea | |
4.1.99.12 | Zn2+ | binding structure, overview | Pyricularia grisea |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.99.12 | D-ribulose 5-phosphate | Pyricularia grisea | - |
formate + L-3,4-dihydroxy-2-butanone-4-phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.99.12 | Pyricularia grisea | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.1.99.12 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.99.12 | D-ribulose 5-phosphate | - |
Pyricularia grisea | formate + L-3,4-dihydroxy-2-butanone-4-phosphate | - |
? | |
4.1.99.12 | 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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.99.12 | dimer | determination of the active sites in the homodimer, crystal structure, overview | Pyricularia grisea |