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Literature summary extracted from

  • Benoni, R.; Pertinhez, T.A.; Spyrakis, F.; Davalli, S.; Pellegrino, S.; Paredi, G.; Pezzotti, A.; Bettati, S.; Campanini, B.; Mozzarelli, A.
    Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR (2016), FEBS Lett., 590, 943-953.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.47 drug development since mammals lack OASS, the enzyme is a potential target for antimicrobial agents Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 drug development since mammals lack OASS, the enzyme is a potential target for antimicrobial agents Haemophilus influenzae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.47 gene cysK, recombinant expression of N-terminal His-tagged enzyme Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 gene cysK, recombinant expression of N-terminal His-tagged enzyme Haemophilus influenzae
2.5.1.47 gene cysM, recombinant expression of N-terminal His-tagged enzyme Salmonella enterica subsp. enterica serovar Typhimurium

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.47 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
2.5.1.47 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
2.5.1.47 additional information anions, like sulfate, significantly reduce the affinity of peptides for CysK Salmonella enterica subsp. enterica serovar Typhimurium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.47 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
2.5.1.47 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Salmonella enterica subsp. enterica serovar Typhimurium
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Haemophilus influenzae
-
 L-cysteine + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Haemophilus influenzae P45040 CysK; gene cysK
-
2.5.1.47 Salmonella enterica subsp. enterica serovar Typhimurium P0A1E3 CysK; gene cysK
-
2.5.1.47 Salmonella enterica subsp. enterica serovar Typhimurium P29848 CysM; gene cysM
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.47 recombinant N-terminal His-tagged enzyme, cleavage and removal of the tag Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 recombinant N-terminal His-tagged enzyme, cleavage and removal of the tag Haemophilus influenzae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Salmonella enterica subsp. enterica serovar Typhimurium L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Haemophilus influenzae L-cysteine + acetate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.47 cysK
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 cysK
-
 Haemophilus influenzae
2.5.1.47 CysM
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 O-acetylserine sulfhydrylase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 O-acetylserine sulfhydrylase
-
 Haemophilus influenzae
2.5.1.47 OASS
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 OASS
-
 Haemophilus influenzae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.47 20
-
 assay at Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 20
-
 assay at Haemophilus influenzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.47 8
-
 assay at Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 8
-
 assay at Haemophilus influenzae