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Literature summary for 2.5.1.47 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)

Cloned (Comment) Organism
-
Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
CysK1
-
Mycobacterium tuberculosis
O-acetylserine sulfhydrylase
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Mycobacterium tuberculosis

Cofactor

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