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Literature summary for 2.5.1.47 extracted from

  • Zocher, G.; Wiesand, U.; Schulz, G.E.
    High resolution structure and catalysis of O-acetylserine sulfhydrylase isozyme B from Escherichia coli (2007), FEBS J., 274, 5382-5389.
    View publication on PubMed
Search for more literature for 2.5.1.47

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with substrate analog citrate, at 1.33 A resolution. The C1-carboxylate of citrate is bound at the carboxylate position of O-acetylserine, whereas the C6-carboxylate adopts two conformations. Modeling of the unnatural substrate 5-thio-2-nitrobenzoate into the structure Escherichia coli

Protein Variants

Protein Variants Comment Organism
Q140E inactive Escherichia coli
Q240A ratio kcat to Km value is 0.4% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy Escherichia coli
R210A ratio kcat to Km value is 2% of wild-type Escherichia coli
T68A ratio kcat to Km value is 0.1% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy Escherichia coli
T68S ratio kcat to Km value is 55% of wild-type Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
 O-acetyl-L-serine mutant T68S, 37°C Escherichia coli
0.7
-
 O-acetyl-L-serine wild-type, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
-
 Escherichia coli ? + acetate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
11
-
 O-acetyl-L-serine mutant T68S, 37°C Escherichia coli
24
-
 O-acetyl-L-serine wild-type, 37°C Escherichia coli