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Literature summary extracted from
- Structure and plasticity of the peptidyl-prolyl isomerase Par27 of Bordetella pertussis revealed by X-ray diffraction and small-angle X-ray scattering (2010), J. Struct. Biol., 169, 253-265.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.2.1.8 | expression of the C-terminally His-tagged Par27 | Bordetella pertussis |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.2.1.8 | purified recombinant His-tagged and SeMet-labeled enzyme, X-ray diffraction structure determination and analysis at 2.2-2.3 A resolution, homology modeling | Bordetella pertussis |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 5.2.1.8 | periplasm | - |
Bordetella pertussis | - |
- |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.2.1.8 | Bordetella pertussis | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.2.1.8 | recombinant C-terminally His-tagged Par27 by nickel affinty chromatography and gel filtration to homogeneity | Bordetella pertussis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.2.1.8 | additional information | Par27 exhibits both chaperone and PPIase activities in vitro. Full-length and isolated PPIase domain show PPIase activity using either reduced carboxymethylated RNAse T1 or a 16-mer peptide as substrates, product analysis by NMR, overview. Functional analysis of enzyme domains and structure modeling, overview | Bordetella pertussis | ? | - |
? |  |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.2.1.8 | dimer | Par27 is the first identified parvulin protein that forms dimers in solution. Par27 is a tripartite protein with a central PPIase domain surrounded by N- and C-terminal sub-domains, NTD and CTD. Par27 structure analysis by X-ray crystallography, small-angle X-ray scattering and template-based modeling, rigid-body modeling, overview | Bordetella pertussis |
| 5.2.1.8 | More | the variability in the orientation of the PPIase domains relative to the NTD/CTD core platform, inter-domain flexibility can be important for the biological activity of this protein. Small angle X-ray and neutron scattering, molecular dynamics simulation, and homology modeling, overview | Bordetella pertussis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.2.1.8 | Par27 | - |
Bordetella pertussis |
| 5.2.1.8 | peptidyl-prolyl isomerase | - |
Bordetella pertussis |
| 5.2.1.8 | PPIase | - |
Bordetella pertussis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.2.1.8 | 20 | - |
assay at | Bordetella pertussis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.2.1.8 | 6.6 | - |
assay at | Bordetella pertussis |
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