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Literature summary for 2.4.1.345 extracted from
- Molecular recognition and interfacial catalysis by the essential phosphatidylinositol mannosyltransferase PimA from mycobacteria (2007), J. Biol. Chem., 282, 20705-20714.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | PimA attaches to the membrane through its N-terminal domain and this association leads to enzyme activation | Mycolicibacterium smegmatis | |
| phospholipid aggregates | the protein is able to interact with mono-disperse phosphatidylinositol through its active site cleft and also with phospholipid aggregates (micelles or liposomes), possibly through a different region of the protein. The latter interactions stimulate the catalytic activity | Mycolicibacterium smegmatis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Mycolicibacterium smegmatis |
| expressed in Escherichia coli | Mycolicibacterium smegmatis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structures of PimA in complex with GDP and GDP-Man are determined using multiplewavelength anomalous diffraction methods at 2.4 A and 2.6 A resolution respectively | Mycolicibacterium smegmatis |
| crystal structures of PimA in complex with GDP and GDP-Man is determined using multiple-wavelength anomalous diffraction methods at 2.4 and 2.6 A of resolution, respectively | Mycolicibacterium smegmatis |
| in complex with GDP and GDP-Man, to 2.4 and 2.6 A resolution, respectively. The structure of PimA in complex with GDP-mannose shows the two-domain organization and the catalytic machinery typical of GT-B glycosyltransferases. Model wherein PimA attaches to the membrane through its N-terminal domain, and this association leads to enzyme activation | Mycolicibacterium smegmatis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| DELTA59-70 | mutation of the beta3-beta2 loop: mutant enzyme is still able to bind GDP with affinities in the submicromolar but PimA is completely inactivated and the ability of the protein to bind phospholipid aggregates is drastically impaired | Mycolicibacterium smegmatis |
| E274A | mutation results in complete enzyme inactivation | Mycolicibacterium smegmatis |
| H118A | mutation results in complete enzyme inactivation | Mycolicibacterium smegmatis |
| additional information | a PimA mutant in which the beta3-alpha2 loop is deleted by mutagenesis (PimA5970) is still able to bind GDP with affinities in the submicromolar range but inactive and impaired the abilityto bind phospholipid aggregates | Mycolicibacterium smegmatis |
| R201A | mutation results in complete enzyme inactivation | Mycolicibacterium smegmatis |
| R77S/K78S/K80S/K81S | mutation of the four basic residues on alpha-helix 2: mutant enzyme is still able to bind GDP with affinities in the submicromolar but PimA is completely inactivated and the ability of the protein to bind phospholipid aggregates is drastically impaired | Mycolicibacterium smegmatis |
| R77S/K78S/K80S/K81S | mutant is still able to bind GDP with affinities in the submicromolar range but inactive and impaired the ability to bind phospholipid aggregates | Mycolicibacterium smegmatis |
| T126W | ability to produce phosphatidylinositol monomannoside (PIM1) is retained, enzymatic activity is similar to wild-type | Mycolicibacterium smegmatis |
| T9A | mutation results in complete enzyme inactivation | Mycolicibacterium smegmatis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | PimA attaches to the membrane through its N-terminal domain and this association leads to enzyme activation | Mycolicibacterium smegmatis | 16020 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GDP-mannose + phosphatidylinositol | Mycolicibacterium smegmatis | PimA is responsible for the initial mannosylation of phosphatidylinositol | GDP + phosphatidyl-(2-O-alpha-D-manno-pyranosyl)-myo-inositol | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycolicibacterium smegmatis | - |
- |
- |
| Mycolicibacterium smegmatis | A0QWG6 | - |
- |
| Mycolicibacterium smegmatis ATCC 700084 | A0QWG6 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| GDP-alpha-D-mannopyranose + 1-acyl-3-(2-(6-O-acyl-alpha-D-mannopyranosyl)-1D-myo-inositolphospho)-2-acyl-sn-glycerol = GDP + 1-acyl-3-(2-(6-O-acyl-alpha-D-mannopyranosyl)-6-O-alpha-D-mannopyranosyl-1D-myo-inositolphospho)-2-acyl-sn-glycerol | based on structural, calorimetric, and mutagenesis studies, a model is proposed wherein PimA attaches to the membrane through its N-terminal domain, and this association leads to enzyme activation | Mycolicibacterium smegmatis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
enzymatic activity is significantly increased using 1,2-dioctanoyl-sn-glycero-3-phospho-inositol as a substrate | Mycolicibacterium smegmatis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GDP-mannose + 1,2-dioctanoyl-sn-glycero-3-phosphoinositol | - |
Mycolicibacterium smegmatis | ? | - |
? | |
| GDP-mannose + phosphatidylinositol | - |
Mycolicibacterium smegmatis | GDP + phosphatidyl-(2-O-alpha-D-manno-pyranosyl)-myo-inositol | - |
? | |
| GDP-mannose + phosphatidylinositol | PimA is responsible for the initial mannosylation of phosphatidylinositol | Mycolicibacterium smegmatis | GDP + phosphatidyl-(2-O-alpha-D-manno-pyranosyl)-myo-inositol | - |
? | |
| GDP-mannose + phosphatidylinositol | - |
Mycolicibacterium smegmatis | GDP + phosphatidyl-(2-O-alpha-D-mannopyranosyl)-myo-inositol | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PimA | - |
Mycolicibacterium smegmatis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mycolicibacterium smegmatis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Mycolicibacterium smegmatis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the stoichiometry of the enzyme-substrate complex strongly depends on phosphatidylinositol concentration. The protein is able to interact with mono-disperse phosphatidylinositol through its active site cleft and also with phospholipid aggregates (micelles or liposomes), possibly through a different region of the protein. The latter interactions stimulate the catalytic activity | Mycolicibacterium smegmatis |
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