Cloned (Comment) | Organism |
---|---|
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) | Pseudomonas aeruginosa |
Crystallization (Comment) | Organism |
---|---|
purified recombinant detagged enzyme, hanging drop vapor diffusion and microseeding techniques, 1.3 to 1.4 M sodium/potassium tartrate and 100 mM HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling | Pseudomonas aeruginosa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Pseudomonas aeruginosa | bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | phosphorylation of conserved catalytic active site residue Ser108 has broad effects on residues in multiple domains. Dephosphorylation of the enzyme may play two critical functional roles: a direct role in the chemical step of phosphoryl transfer and secondly through propagation of structural flexibility. Dephosphorylation has minimal effects on crystal structure of the enzyme | Pseudomonas aeruginosa |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag, purification by nickel affinity chromatography and dialysis | Pseudomonas aeruginosa |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate | acid-base catalysis mechanism, key role for conformational change in its multistep reaction, which requires a dramatic 180 degree reorientation of the intermediate within the active site. Modeling shows that increased enzyme flexibility facilitates the reorientation of the reaction intermediate, coupling changes in structural dynamics with the unique catalytic mechanism of this enzyme | Pseudomonas aeruginosa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities | Pseudomonas aeruginosa | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structure analysis of the active phosphoenzyme, the inactive dephosphoenzyme, and the phosphoenzyme in complex with the substrate analog xylose 1-phosphate, overview | Pseudomonas aeruginosa |
Synonyms | Comment | Organism |
---|---|---|
phosphomannomutase/phosphoglucomutase | - |
Pseudomonas aeruginosa |
PMM/PGM | - |
Pseudomonas aeruginosa |
General Information | Comment | Organism |
---|---|---|
additional information | analysis of conformational flexibility of different forms of phosphoglucomutase/phosphomannomutase in solution, including its active, phosphorylated state and the unphosphorylated state that occurs transiently during the catalytic cycle, by hydrogen-deuterium exchange by mass spectrometry and small angle x-ray scattering. Both ligand binding and phosphorylation of the catalytic phosphoserine affect the overall flexibility of the enzyme in solution | Pseudomonas aeruginosa |
physiological function | the enzyme catalyzes an intramolecular phosphoryl transfer across its phosphosugar substrates, which are precursors in the synthesis of exoproducts involved in bacterial virulence | Pseudomonas aeruginosa |