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Literature summary 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)

EC Number Crystallization (Comment) Organism
2.5.1.47 to 2.2 A resolution Bacillus anthracis
4.2.1.22 to 2.2 A resolution Bacillus anthracis

Protein Variants

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.47 1.168
-
 O-acetyl-L-serine wild-type, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 1.65
-
 O-acetyl-L-serine mutant A72S, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 2.05
-
 O-acetyl-L-serine mutant E220R, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 6.18
-
 O-acetyl-L-serine production of H2S, wild-type, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 9.01
-
 O-acetyl-L-serine production of H2S, mutant A72S, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 0.32
-
 L-homocysteine wild-type, production of H2S, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 1.51
-
 L-homocysteine mutant E220R, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 2.73
-
 L-homocysteine wild-type, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 3.59
-
 L-homocysteine mutant A72S, pH 8.2, 37°C Bacillus anthracis

Organism

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.5.1.47 ? x * 31400, SDS-PAGE Bacillus anthracis
4.2.1.22 ? x * 31400, SDS-PAGE Bacillus anthracis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.47 0.7
-
 O-acetyl-L-serine production of H2S, wild-type, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 0.9
-
 O-acetyl-L-serine production of H2S, mutant A72S, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 4.46
-
 O-acetyl-L-serine wild-type, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 4.88
-
 O-acetyl-L-serine mutant A72S, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 5.46
-
 O-acetyl-L-serine mutant E220R, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 3.38
-
 L-homocysteine wild-type, production of H2S, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 5.74
-
 L-homocysteine mutant E220R, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 8.39
-
 L-homocysteine wild-type, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 10.91
-
 L-homocysteine mutant A72S, pH 8.2, 37°C Bacillus anthracis

Cofactor

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.47 0.1
-
 O-acetyl-L-serine production of H2S, mutant A72S, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 0.11
-
 O-acetyl-L-serine production of H2S, wild-type, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 2.67
-
 O-acetyl-L-serine mutant E220R, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 2.96
-
 O-acetyl-L-serine mutant A72S, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 3.82
-
 O-acetyl-L-serine wild-type, pH 8.2, 37°C Bacillus anthracis
2.5.1.47 10.56
-
 L-homocysteine wild-type, production of H2S, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 3.04
-
 L-homocysteine mutant A72S, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 3.06
-
 L-homocysteine wild-type, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 3.83
-
 L-homocysteine mutant E220R, pH 8.2, 37°C Bacillus anthracis
4.2.1.22 10.56
-
 L-homocysteine wild-type, production of H2S, pH 8.2, 37°C Bacillus anthracis