EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.88 | recombinant overexpression of C-terminally His6-tagged enzyme in Escherichia coli strain C41 (DE3) | Staphylococcus aureus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.5.1.88 | purified recombinant His6-tagged enzyme in complex with four hydroxamate inhibitors, hanging drop vapour-diffusion method, mixing of 30 mg/ml protein in 20 mM Tris-HCl, pH 7.5, and 120 mM NaCl, with reservoir solution consisting of 23% w/v PEG 4000, 50 mM Tris-HCl pH 8.5, 15% v/v glycerol, 100 mM MgCl2, 20mM CaCl2, X-ray diffraction structure determination and analysis at resolutions of 1.90-2.30 A | Staphylococcus aureus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.88 | (2R)-N-[(2S)-1-{4-[(2H-1,3-benzodioxol-5-yl)methyl]piperazin-1-yl}-3,3-dimethyl-1-oxobutan-2-yl]-2-(cyclopentylmethyl)-3-[formyl(hydroxy)amino]propanamide | - |
Staphylococcus aureus | |
3.5.1.88 | actinonin | - |
Staphylococcus aureus | |
3.5.1.88 | additional information | effects of inhibitors on the enzyme structure, overview | Staphylococcus aureus | |
3.5.1.88 | N-(5-fluoro-1-hydroxypyridin-1-ium-2-yl)-1-[(2R)-2-[[formyl(hydroxy)amino]methyl]hexanoyl]prolinamide | - |
Staphylococcus aureus | |
3.5.1.88 | N-[(2-methoxyphenyl)carbamoyl]-3-methyl-L-valyl-N2-(cyclopentylmethyl)-N-hydroxyglycinamide | binding structure, overview | Staphylococcus aureus | |
3.5.1.88 | N-[(2R,4S)-2-butyl-4-[[(2-fluorophenyl)carbamoyl]amino]-5-methyl-3-oxohexyl]-N-hydroxyformamide | binding structure, overview | Staphylococcus aureus | |
3.5.1.88 | N-[(2R,4S)-2-butyl-5-methyl-4-[[(5-methylpyridin-2-yl)carbamoyl]amino]-3-oxohexyl]-N-hydroxyformamide | binding structure, overview | Staphylococcus aureus | |
3.5.1.88 | N-[(3,5-difluorophenyl)carbamoyl]-3-methyl-L-valyl-N2-(cyclopentylmethyl)-N-hydroxyglycinamide | binding structure, overview | Staphylococcus aureus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.88 | Zn2+ | a zinc-metalloenzyme | Staphylococcus aureus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.88 | Staphylococcus aureus | - |
- |
- |
3.5.1.88 | Staphylococcus aureus ATCC 6538p | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.1.88 | recombinant C-terminally His6-tagged enzyme from Escherichia coli strain C41 (DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration | Staphylococcus aureus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.88 | formyl-Met-Ala-Ser + H2O | - |
Staphylococcus aureus | formate + Met-Ala-Ser | - |
? | |
3.5.1.88 | formyl-Met-Ala-Ser + H2O | - |
Staphylococcus aureus ATCC 6538p | formate + Met-Ala-Ser | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.88 | - |
Staphylococcus aureus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.88 | 9.5 | - |
assay at | Staphylococcus aureus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.88 | 0.0000112 | - |
N-[(2R,4S)-2-butyl-5-methyl-4-[[(5-methylpyridin-2-yl)carbamoyl]amino]-3-oxohexyl]-N-hydroxyformamide | pH 7.0, temperature not specified in the publication | Staphylococcus aureus | |
3.5.1.88 | 0.0000351 | - |
N-[(2R,4S)-2-butyl-4-[[(2-fluorophenyl)carbamoyl]amino]-5-methyl-3-oxohexyl]-N-hydroxyformamide | pH 7.0, temperature not specified in the publication | Staphylococcus aureus | |
3.5.1.88 | 0.0000524 | - |
N-[(3,5-difluorophenyl)carbamoyl]-3-methyl-L-valyl-N2-(cyclopentylmethyl)-N-hydroxyglycinamide | pH 7.0, temperature not specified in the publication | Staphylococcus aureus | |
3.5.1.88 | 0.0000849 | - |
N-[(2-methoxyphenyl)carbamoyl]-3-methyl-L-valyl-N2-(cyclopentylmethyl)-N-hydroxyglycinamide | pH 7.0, temperature not specified in the publication | Staphylococcus aureus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.88 | physiological function | peptide deformylase catalyzes the removal of the formyl group from the N-terminal methionine residue in newly synthesized polypeptides, which is an essential process in bacteria | Staphylococcus aureus |