EC Number   |
Inhibitors |
Structure  |
|---|
    2.5.1.47 | more |
partial inhibition of enzyme upon complex formation with serine acetyltransferase |
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| 2.5.1.47 | more |
presence of 4% NaCl is not inhibitory |
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| 2.5.1.47 | more |
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction |
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| 2.5.1.47 | more |
CysK is competitively inhibited within the cysteine synthase complex |
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| 2.5.1.47 | more |
molecular dynamic simulation and inhibitor prediction of cysteine synthase |
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| 2.5.1.47 | more |
anions, like sulfate, significantly reduce the affinity of peptides for CysK |
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| 2.5.1.47 | more |
identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors; identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors, no inhibition of isozyme CS3 by exophillic acid from Exophiala sp.FKI-7082, which is specific for isozyme CS1 |
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| 2.5.1.47 | more |
rational structure-guided design of nanomolar thiazolidine inhibitors of Mycobacterium tuberculosis CysK1 O-acetyl serine sulfhydrylase, discovered using the crystal structure of a CysK1-peptide inhibitor complex as template, pharmacophore modeling and in vitro screening, overview. Chemical synthesis leads to improved thiazolidine inhibitors with an IC50 value of 19 nM for the best compound, a 150fold higher potency than the natural peptide inhibitor with IC50 of 0.0029 mM |
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| 2.5.1.47 | more |
computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview; computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview |
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| 2.5.1.47 | more |
enzyme inhibitor development, in silico molecular docking simulations, using the three-dimensional crystal structure of O-acetyl-L-serine sulfhydrylase enzyme complexed with cysteine and pyridoxal 5'-phosphate ligands, PDB ID 3BM5, on nine pyrazolo[3,4-d]pyrimidine molecules without linkers and nine pyrazolo[3,4-d]pyrimidine molecules with a trimethylene linker along with the reference drug metronidazole, binding structures, ligand docking and interaction analysis, detiled overview |
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