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Literature summary for 2.5.1.47 extracted from
- Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR (2016), FEBS Lett., 590, 943-953.
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | since mammals lack OASS, the enzyme is a potential target for antimicrobial agents | Salmonella enterica subsp. enterica serovar Typhimurium |
| drug development | since mammals lack OASS, the enzyme is a potential target for antimicrobial agents | Haemophilus influenzae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene cysK, recombinant expression of N-terminal His-tagged enzyme | Salmonella enterica subsp. enterica serovar Typhimurium |
| gene cysK, recombinant expression of N-terminal His-tagged enzyme | Haemophilus influenzae |
| gene cysM, recombinant expression of N-terminal His-tagged enzyme | Salmonella enterica subsp. enterica serovar Typhimurium |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| MNYDI | interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview | Haemophilus influenzae |  |
| MNYDI | interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview; interaction of the inhibitory pentapeptide MNYDI with CysM OASS isozyme from Salmonella typhimurium, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview. In isozyme CysM multiple H-bond interactions are made by Asn2 side chain with S205 side chain and I206 and I209 backbone carbonyl groups | Salmonella enterica subsp. enterica serovar Typhimurium | |
| additional information | anions, like sulfate, significantly reduce the affinity of peptides for CysK | Salmonella enterica subsp. enterica serovar Typhimurium |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | important role of the C-terminal residue Ile5 and the arylic moiety at P3 in dictating enzyme affinity, dissociation constant of MNYDI | Salmonella enterica subsp. enterica serovar Typhimurium | |
| additional information | - |
additional information | important role of the C-terminal residue Ile5 and the arylic moiety at P3 in dictating enzyme affinity, dissociation constant of MNYDI | Haemophilus influenzae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| O-acetyl-L-serine + hydrogen sulfide | Salmonella enterica subsp. enterica serovar Typhimurium | - |
L-cysteine + acetate | - |
? | |
| O-acetyl-L-serine + hydrogen sulfide | Haemophilus influenzae | - |
L-cysteine + acetate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haemophilus influenzae | P45040 | CysK; gene cysK | - |
| Salmonella enterica subsp. enterica serovar Typhimurium | P0A1E3 | CysK; gene cysK | - |
| Salmonella enterica subsp. enterica serovar Typhimurium | P29848 | CysM; gene cysM | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminal His-tagged enzyme, cleavage and removal of the tag | Salmonella enterica subsp. enterica serovar Typhimurium |
| recombinant N-terminal His-tagged enzyme, cleavage and removal of the tag | Haemophilus influenzae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| O-acetyl-L-serine + hydrogen sulfide | - |
Salmonella enterica subsp. enterica serovar Typhimurium | L-cysteine + acetate | - |
? | |
| O-acetyl-L-serine + hydrogen sulfide | - |
Haemophilus influenzae | L-cysteine + acetate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cysK | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| cysK | - |
Haemophilus influenzae |
| CysM | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| O-acetylserine sulfhydrylase | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| O-acetylserine sulfhydrylase | - |
Haemophilus influenzae |
| OASS | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| OASS | - |
Haemophilus influenzae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
assay at | Salmonella enterica subsp. enterica serovar Typhimurium |
| 20 | - |
assay at | Haemophilus influenzae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Salmonella enterica subsp. enterica serovar Typhimurium |
| 8 | - |
assay at | Haemophilus influenzae |
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