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Literature summary for 2.5.1.47 extracted from

  • Chinthalapudi, K.; Kumar, M.; Kumar, S.; Jain, S.; Alam, N.; Gourinath, S.
    Crystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: structural evidence for cysteine binding and lack of interactions with serine acetyl transferase (2008), Proteins, 72, 1222-1232.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BLR with pET-28a Entamoeba histolytica

Crystallization (Commentary)

Crystallization (Comment) Organism
native and in complex with its product L-cysteine, 50 mM Tris buffer, pH 8.0, with 150 mM NaCl, hanging drop method at 16°C, 2.3 M ammonium sulfate as precipitant for the complex with 5 mM cysteine in 100 mM Tris, pH 7.2, with increasing glycerol concentrations, diffraction data collection at -173°C Entamoeba histolytica
native protein at 1.86 A resolution, in complex with product cysteine at 2.4 A resolution. The dimeric interface lacks a chloride binding site. The N-terminal extension participates in dimeric interactions in a domain swapping manner. Sulfate is bound in the active site of the native structure, which is replaced by cysteine in the cysteine bound form Entamoeba histolytica

General Stability

General Stability Organism
extended dimeric interface interactions contribute to the stability of the dimer under physiological conditions Entamoeba histolytica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O3-acetyl-L-serine + hydrogen sulfide Entamoeba histolytica in the absence of sulfide O3-acetyl-L-serine reacts with the cofactor pyridoxal 5'-phosphate to alpha-aminoacrylate intermediate L-cysteine + acetate
-
?

Organism

Organism UniProt Comment Textmining
Entamoeba histolytica
-
-
-
Entamoeba histolytica O15570
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-

Purification (Commentary)

Purification (Comment) Organism
-
Entamoeba histolytica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O3-acetyl-L-serine + hydrogen sulfide in the absence of sulfide O3-acetyl-L-serine reacts with the cofactor pyridoxal 5'-phosphate to alpha-aminoacrylate intermediate Entamoeba histolytica L-cysteine + acetate
-
?

Subunits

Subunits Comment Organism
dimer crystallization data Entamoeba histolytica
dimer 2 * ?, determined by molecular replacement of crystal structure Entamoeba histolytica

Synonyms

Synonyms Comment Organism
EhOASS
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Entamoeba histolytica
O-acetylserine sulfhydrylase
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Entamoeba histolytica

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate gives the crystals a yellow color, covalently linked to Lys58, interaction with Gly236, Ser280, Pro307, cofactor orientation at the active site and absorbance maximum change upon binding of cysteine or methionine Entamoeba histolytica

General Information

General Information Comment Organism
physiological function product cysteine plays an important role in the antioxidative defense mechanisms of the human parasite Entamoeba histolytica