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Literature summary for 3.5.1.88 extracted from
- Purification and use of E. coli peptide deformylase for peptide deprotection in chemoenzymatic peptide synthesis (2013), Protein Expr. Purif., 89, 73-79.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme is an attractive candidate for the biocatalytic deprotection of formylated peptides that are used in chemoenzymatic peptide synthesis | Escherichia coli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene def, recombinant expression of the enzyme fused to an octaglutamate tag using expression vector pBAD/Myc-His-DEST in Escherichia coli TOP10 cells and strain JM109 | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | fusion of the enzyme to an octaglutamate tag-deformylation activity and stability of the engineered enzyme are similar to those of the wild-type | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 19000 | - |
1 * 19000, SDS-PAGE | Escherichia coli |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| N,N-dimethylformamide | inactivates the enzyme at 10%, DMSO and methanol at about 40% | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A6K3 | gene def | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme 8.2fold by Met-Lys affinity chromatography, recombinant enzyme fused to an octaglutamate tag 5-5.5fold by two different methods of anion exchange chromatography, ultrafiltration, and gel filtration, deformylation activity and stability of the engineered enzyme are similar to those of the wild-type | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 229 | - |
recombinant wild-type enzyme, cell-free extract from overexpressing cell culture, pH 7.2, 30°C | Escherichia coli |
| 884 | 970 | purified recombinant engineered enzyme, pH 7.2, 30°C | Escherichia coli |
| 1880 | - |
purified recombinant wild-type enzyme, pH 7.2, 30°C | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| formyl-Met-Ala + H2O | - |
Escherichia coli | formate + Met-Ala | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 19000, SDS-PAGE | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
- |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | peptide deformylases catalyze the removal of the formyl group from the N-terminal methionine residue in nascent polypeptide chains in prokaryotes | Escherichia coli |
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Release 2023.1 (January 2023)
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