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Literature summary extracted from

  • Schnell, R.; Oehlmann, W.; Singh, M.; Schneider, G.
    Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis: Crystal structures of the enzyme - alpha -aminoacrylate intermediate and an enzyme-inhibitor complex (2007), J. Biol. Chem., 282, 23473-23481.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.47
-
 Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.47 trapping of the alpha-aminoacrylate reaction intermediate and determination of its structure by cryocrystallography, 2.2 A resolution. Determination of the crystal structure of the enzyme bound to an inhibitory four-residue peptide derived from the C-terminus of Mycobacterium tuberculosis CysE (SAT, Rv2335). The structure of this inhibited form of CysK1 may provide the basis for the design of strong binding inhibitors of this enzyme Mycobacterium tuberculosis

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.47 O-acetyl-L-Ser + H2S
-
 Mycobacterium tuberculosis L-Cys + acetate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.47 CysK1
-
 Mycobacterium tuberculosis
2.5.1.47 O-acetylserine sulfhydrylase
-
 Mycobacterium tuberculosis

Cofactor

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