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Literature summary for 2.5.1.47 extracted from

  • Devi, S.; Abdul Rehman, S.A.; Tarique, K.F.; Gourinath, S.
    Structural characterization and functional analysis of cystathionine beta-synthase an enzyme involved in the reverse transsulfuration pathway of Bacillus anthracis (2017), FEBS J., 284, 3862-3880 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
to 2.2 A resolution Bacillus anthracis

Protein Variants

Protein Variants Comment Organism
A72S mutant produces more H2S than wild-type Bacillus anthracis
E220R not able to release H2S Bacillus anthracis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.168
-
O-acetyl-L-serine wild-type, pH 8.2, 37°C Bacillus anthracis
1.65
-
O-acetyl-L-serine mutant A72S, pH 8.2, 37°C Bacillus anthracis
2.05
-
O-acetyl-L-serine mutant E220R, pH 8.2, 37°C Bacillus anthracis
6.18
-
O-acetyl-L-serine production of H2S, wild-type, pH 8.2, 37°C Bacillus anthracis
9.01
-
O-acetyl-L-serine production of H2S, mutant A72S, pH 8.2, 37°C Bacillus anthracis

Organism

Organism UniProt Comment Textmining
Bacillus anthracis A0A1J9VES8 enzyme shows activities of both EC 4.2.1.22 and 2.5.1.47
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + H2O
-
Bacillus anthracis L-serine + H2S
-
?
L-cysteine + L-homocysteine
-
Bacillus anthracis L-cystathionine + H2S
-
?
additional information no substrate: L-serine Bacillus anthracis ?
-
?
O-acetyl-L-serine
-
Bacillus anthracis L-cysteine + acetate
-
?
O-acetyl-L-serine + H2S
-
Bacillus anthracis L-cysteine + acetic acid
-
?

Subunits

Subunits Comment Organism
? x * 31400, SDS-PAGE Bacillus anthracis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.7
-
O-acetyl-L-serine production of H2S, wild-type, pH 8.2, 37°C Bacillus anthracis
0.9
-
O-acetyl-L-serine production of H2S, mutant A72S, pH 8.2, 37°C Bacillus anthracis
4.46
-
O-acetyl-L-serine wild-type, pH 8.2, 37°C Bacillus anthracis
4.88
-
O-acetyl-L-serine mutant A72S, pH 8.2, 37°C Bacillus anthracis
5.46
-
O-acetyl-L-serine mutant E220R, pH 8.2, 37°C Bacillus anthracis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate cofactor is highly flexible due to the active site being wide open Bacillus anthracis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.1
-
O-acetyl-L-serine production of H2S, mutant A72S, pH 8.2, 37°C Bacillus anthracis
0.11
-
O-acetyl-L-serine production of H2S, wild-type, pH 8.2, 37°C Bacillus anthracis
2.67
-
O-acetyl-L-serine mutant E220R, pH 8.2, 37°C Bacillus anthracis
2.96
-
O-acetyl-L-serine mutant A72S, pH 8.2, 37°C Bacillus anthracis
3.82
-
O-acetyl-L-serine wild-type, pH 8.2, 37°C Bacillus anthracis
10.56
-
L-homocysteine wild-type, production of H2S, pH 8.2, 37°C Bacillus anthracis