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Literature summary for 5.4.2.2 extracted from
- Identification of an essential active-site residue in the alpha-D-phosphohexomutase enzyme superfamily (2013), FEBS J., 280, 2622-2632.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), expression of untagged mutant H329A in Escherichia coli strain BL21(DE3) | Pseudomonas aeruginosa |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant untagged enzyme mutant H329A, from 1.2-1.6 M Na,K tartrate and 100 mM Na HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling | Pseudomonas aeruginosa |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H329A | site-directed mutagenesis, crystal structure determination and comparison, the mutant shows no significant changes from the wild-type enzyme, excluding structural disruption as the source of its compromised activity. The kcat of the mutant is 3000fold reduced relative to the wild-type enzyme | Pseudomonas aeruginosa |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten steady-state kinetics of wild-type and mutant H329A enzymes, overview | Pseudomonas aeruginosa | |
| 0.03 | - |
alpha-D-glucose 1-phosphate | mutant H329A, pH 7.5, temperature not specified in the publication | Pseudomonas aeruginosa |  |
| 0.08 | - |
alpha-D-glucose 1-phosphate | wild-type enzyme, pH 7.5, temperature not specified in the publication | Pseudomonas aeruginosa | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Pseudomonas aeruginosa | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-glucose 1-phosphate | Pseudomonas aeruginosa | - |
D-glucose 6-phosphate | - |
r | |
| additional information | Pseudomonas aeruginosa | bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities. Strongly conserved residue His329 in the active site is critical for enzyme activity. His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | phosphorylation of active site Ser108 in wild-type and mutant enzymes | Pseudomonas aeruginosa |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant untagged mutant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography and dialysis, recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Pseudomonas aeruginosa |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| alpha-D-glucose 1-phosphate = D-glucose 6-phosphate | acid-base catalysis mechanism, overview. His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-glucose 1-phosphate | - |
Pseudomonas aeruginosa | D-glucose 6-phosphate | - |
r | |
| additional information | bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities. Strongly conserved residue His329 in the active site is critical for enzyme activity. His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction | Pseudomonas aeruginosa | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| phosphomannomutase/phosphoglucomutase | - |
Pseudomonas aeruginosa |
| PMM/PGM | - |
Pseudomonas aeruginosa |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.03 | - |
alpha-D-glucose 1-phosphate | mutant H329A, pH 7.5, temperature not specified in the publication | Pseudomonas aeruginosa | |
| 95 | - |
alpha-D-glucose 1-phosphate | wild-type enzyme, pH 7.5, temperature not specified in the publication | Pseudomonas aeruginosa | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | 8 | depending on the substrate | Pseudomonas aeruginosa |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the alpha-D-phosphohexomutase enzyme superfamily | Pseudomonas aeruginosa |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1 | - |
alpha-D-glucose 1-phosphate | mutant H329A, pH 7.5, temperature not specified in the publication | Pseudomonas aeruginosa | |
| 1188 | - |
alpha-D-glucose 1-phosphate | wild-type enzyme, pH 7.5, temperature not specified in the publication | Pseudomonas aeruginosa | |
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