Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.47 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
Search for more literature for 2.5.1.47

Application

Application Comment Organism
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

Inhibitors Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O-acetyl-L-serine + hydrogen sulfide Mycobacterium tuberculosis
-
 L-cysteine + acetate
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WP55
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-acetyl-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis L-cysteine + acetate
-
 ?

Synonyms

Synonyms Comment Organism
CysK1
-
 Mycobacterium tuberculosis

Cofactor

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