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Literature summary for 2.8.1.6 extracted from

  • Ollagnier-de-Choudens, S.; Mulliez, E.; Hewitson, K.S.; Fontecave, M.
    Biotin synthase is a pyridoxal phosphate-dependent cysteine desulfurase (2002), Biochemistry, 41, 9145-9152.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol 10fold stimulation of cysteine desulfurase activity of the enzyme at 20 mM Escherichia coli
L-cysteine increases biotin production Escherichia coli
pyridoxal 5'-phosphate required for cysteine desulfurase activity of the enzyme Escherichia coli

Protein Variants

Protein Variants Comment Organism
C128A reduced cysteine desulfurase activity Escherichia coli
C188A cysteine desulfurase activity is reduced to 70% of the wild-type activity Escherichia coli
C97A reduced cysteine desulfurase activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NaBH4 decreases cysteine desulfurase and biotin synthase activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03
-
L-cysteine pH 8, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dethiobiotin + sulfur
-
Escherichia coli biotin
-
?
L-cysteine enzyme displays cysteine desulfurase activity, providing it with the ability to mobilize sulfur from free cysteine Escherichia coli L-alanine + sulfide
-
?