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Literature summary extracted from
- A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation (2016), FEBS J., 283, 4310-4324 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.19.1 | gene aph, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme SpAAP in Escherichia coli | Sporosarcina psychrophila |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.19.1 | purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 50 mM sodium phosphate, 100 mM NaCl, pH 7.5, with 0.001 ml reservoir solution containing 30% PEG 400, 0.1 M Na-HEPES, pH 7.5, 0.2 M MgCl2, and 0.1 M (NH4)2SO4, 4°C, X-ray diffraction structure determination and analysis at 2.5 A resolution | Sporosarcina psychrophila |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | additional information | enzyme mutants lacking the arm in the quarternary structure are monomeric, inactive and highly prone to aggregation | Sporosarcina psychrophila |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.19.1 | Sporosarcina psychrophila | E1VFE0 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.19.1 | recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography | Sporosarcina psychrophila |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | homodimer | release of subunits from the quaternary structure is hindered by an arm exchange mechanism, in which a tiny structural element at the N-terminus of one subunit inserts into the other subunit. Mutants lacking the arm are monomeric, inactive and highly prone to aggregation | Sporosarcina psychrophila |
| 3.4.19.1 | More | tertiary and quarternary structure analysis and tructure comparisons, overview | Sporosarcina psychrophila |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | acyl aminoacyl peptidase | - |
Sporosarcina psychrophila |
| 3.4.19.1 | APH | - |
Sporosarcina psychrophila |
| 3.4.19.1 | SpAAP | - |
Sporosarcina psychrophila |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | additional information | the three-dimensional structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) highlights adaptive molecular changes resulting in a fine-tuned trade-off between flexibility and stability. A feature of SpAAP cold adaptation is the enlargement of the tunnel connecting the exterior of the protein with the active site. Such a wide channel might compensate for the reduced molecular motions occurring in the cold and allow easy and direct access of substrates to the catalytic site, rendering transient movements between domains unnecessary. Thus, cold-adapted SpAAP has developed a molecular strategy unique within this group of proteins: it is able to enhance the flexibility of each functional unit while still preserving sufficient stability. The Ser-Asp-His catalytic triad in SpAAP (Ser458, Asp540 and His572) matches that of the canonical alpha/beta hydrolase fold | Sporosarcina psychrophila |
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