Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

5.3.1.23: S-methyl-5-thioribose-1-phosphate isomerase

This is an abbreviated version!
For detailed information about S-methyl-5-thioribose-1-phosphate isomerase, go to the full flat file.

Word Map on EC 5.3.1.23

Reaction

S-methyl-5-thio-alpha-D-ribose 1-phosphate
=
S-methyl-5-thio-D-ribulose 1-phosphate

Synonyms

1-PMTR isomerase, 5'-methylthioribose-1-phosphate isomerase, 5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase, 5-methylthioribose 1-phosphate isomerase, 5-methylthioribose-1-phosphate isomerase, Bs-M1Pi, Isomerase, methylthioribose 1-phosphate, M1Pi, methylthioribose-1-phosphate isomerase, Meu1p, MRDI, MRI1, Mri1p, mtnA, MTR-1-P, MTR-1-P isomerase, PH0702, PhM1Pi, Ypr118w, Ypr118wp

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.1 Interconverting aldoses and ketoses, and related compounds
                5.3.1.23 S-methyl-5-thioribose-1-phosphate isomerase

Crystallization

Crystallization on EC 5.3.1.23 - S-methyl-5-thioribose-1-phosphate isomerase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallized with the substrate 5-methylthio-5-deoxy-D-ribose 1-phosphate, sitting drop vapour diffusion method, using 0.2 M K formate and 15% (w/v) polyethylene glycol 3350, at 20°C
purified enzyme in complex with product S-methyl-1-thio-D-ribulose 1-phosphate or a sulfate ion, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 50 mM Na HEPES, pH 7.4, and 1 mM EDTA, with or without 33 mM MTR-1-P, with 0.004-0.006 ml of reservoir solution containing 0.2 M K formate and 15% w/v PEG 3350, 20°C, X-ray diffraction structure determination and analysis at 2.4 A and 2.7 A resolution, respectively. The asymmetric unit contains two dimers for the MTRu-1-P-bound form, while one dimer is found in the asymmetric unit for the sulfate-bound form. Molecular replacement method using the crystal structure of Ypr118w (RCSB, PDB ID 1W2W) as a search model, and modeling
sitting-drop vapour-diffusion method. Crystals diffract to 2.5 A at 100 K using synchrotron radiation and belong to the tetragonal space group P4(1), with unit-cell parameters a = b = 69.2 A, c = 154.7 A
-
hanging drop vapor diffusion method, using 0.7 M sodium citrate and 100 mM imidazole, pH 8.0
in silico analysis of conserved residues and molecular modeling of structure. Residues of the enzymic activity of methylthioribose-1-phosphate isomerase that interact with the substrate are absolutely conserved. Residues essential for the hydrophobic stabilization of the substrate/product in the active site are conserved as well
purified recombinant enzyme in two different forms of crystals belonging to space groups P3221 and P1, that are obtained at 4°C and 20°C, respectively. The crystal belonging to space group P3221 grows in a microbatch-under-oil set up by mixing 0.002 ml of protein solution and 0.002 ml of 0.1 M sodium citrate tribasic dihydrate, pH 5.6, and 2.5 M 1,6-hexanediol. Initial crystals belonging to space group P1 are obtained by hanging-drop vapor-diffusion method, mixing of 0.003 ml of protein solution with 0.001 ml of resevoir solution containing 0.05 M ammonium acetate, 0.1 M Tris, pH 8.0, 16% PEG 10000 and 0.05 M sodium acetate, method optimization, X-ray diffraction structure determination analysis at 2.30-2.65 A resolution, molecular replacement method using the three-dimensional atomic coordinates of M1Pi from Archaeoglobus fulgidus (PDB ID 1T5O) as the search model, modeling
sitting-drop vapour-diffusion method
-