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Literature summary extracted from

  • Poyraz, O.; Jeankumar, V.U.; Saxena, S.; Schnell, R.; Haraldsson, M.; Yogeeswari, P.; Sriram, D.; Schneider, G.
    Structure-guided design of novel thiazolidine inhibitors of O-acetyl serine sulfhydrylase from Mycobacterium tuberculosis (2013), J. Med. Chem., 56, 6457-6466.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.47 drug development cysteine biosynthetic pathway is absent in humans but essential in microbial pathogens, suggesting that it provides potential targets for the development of novel antibacterial compounds Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.47 additional information 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 Mycobacterium tuberculosis

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 Mycobacterium tuberculosis
-
L-cysteine + acetate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Mycobacterium tuberculosis P9WP55
-
-

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
-
Mycobacterium tuberculosis L-cysteine + acetate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.47 CysK1
-
Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.47 pyridoxal 5'-phosphate dependent on Mycobacterium tuberculosis