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Literature summary for 5.4.2.8 extracted from
- Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase (2012), Mol. Microbiol., 85, 513-534.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene PMM, DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli | Trypanosoma brucei |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant detagged enzyme, hanging drop vapour diffusion, from 2 M (NH4)2SO4, 0.2 M NaCl, 0.1 M sodium cacodylate, pH 6.0, 20°C, X-ray diffraction structure determination and analysis at 1.86 A resolution, molecular replacement using a modified form of the Leishmania mexicana enzyme, PDB ID 2i54 | Trypanosoma brucei |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | RNAi knockdown of gene TbPMM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview | Trypanosoma brucei |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.327 | - |
alpha-D-mannose 1-phosphate | pH 7.3, 37°C | Trypanosoma brucei |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| glycosome | blood stream parasite form | Trypanosoma brucei | 20015 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-mannose 1-phosphate | Trypanosoma brucei | - |
D-mannose 6-phosphate | - |
? | |
| alpha-D-mannose 1-phosphate | Trypanosoma brucei 427 | - |
D-mannose 6-phosphate | - |
? | |
| additional information | Trypanosoma brucei | the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview | ? | - |
? | |
| additional information | Trypanosoma brucei 427 | the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trypanosoma brucei | F4NCC2 | gene PMM | - |
| Trypanosoma brucei 427 | F4NCC2 | gene PMM | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration, removal of the His-tag by TEV protease | Trypanosoma brucei |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | quantitative proteomic analysis show that the TbPMM protein is present in both life cycle stages, procyclic and bloodstream forms | Trypanosoma brucei | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-mannose 1-phosphate | - |
Trypanosoma brucei | D-mannose 6-phosphate | - |
? | |
| alpha-D-mannose 1-phosphate | - |
Trypanosoma brucei 427 | D-mannose 6-phosphate | - |
? | |
| additional information | the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview | Trypanosoma brucei | ? | - |
? | |
| additional information | the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview | Trypanosoma brucei 427 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PMM | - |
Trypanosoma brucei |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Trypanosoma brucei |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
- |
Trypanosoma brucei |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 8 | activity range, inactive above and below | Trypanosoma brucei |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the alpha-D-phosphohexomutase superfamily of enzymes | Trypanosoma brucei |
| additional information | the cap domain contributes the residues involved in substrate recognition, E119, R121, M124, N126, R132, R139, S177, so that the active site is located in the groove at the interface of the core and cap domains | Trypanosoma brucei |
| physiological function | the enzyme is essential for parasite growth. It takes over the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphoacetylglucosamine mutase, EC 5.4.2.3, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview | Trypanosoma brucei |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 37 | - |
alpha-D-mannose 1-phosphate | pH 7.3, 37°C | Trypanosoma brucei | |
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Release 2023.1 (January 2023)
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