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Literature summary for 2.5.1.47 extracted from

  • Flint, D.H.; Tuminello, J.F.; Miller, T.J.
    Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in escherichia coli crude extract. Isolation of O-acetylserine sulfhydrylases A and B and beta-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis (1996), J. Biol. Chem., 271, 16053-16067.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-Cys + acetate Escherichia coli involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate mechanism of reverse reaction Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 activity depends on presence of nucleophiles Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Cys + acetate
-
 Escherichia coli O-acetyl-L-Ser + H2S
-
 r
L-Cys + acetate involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear Escherichia coli ?
-
 ?
additional information several nucleophiles may stimulate sulfide formation Escherichia coli ?
-
 ?
O-acetyl-L-Ser + H2S
-
 Escherichia coli L-Cys + acetate
-
 r