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Literature summary extracted from

  • Manders, A.L.; Jaworski, A.F.; Ahmed, M.; Aitken, S.M.
    Exploration of structure-function relationships in Escherichia coli cystathionine gamma-synthase and cystathionine beta-lyase via chimeric constructs and site-specific substitutions (2013), Biochim. Biophys. Acta, 1834, 1044-1053.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.4.1.13 expression of wild-type and chimeric mutant enzymes in Escherichia coli strain ER1821, in vivo complementation of methionine-auxotrophic Escherichia coli strains, lacking the genes encoding cystathionine gamma-synthase and cystathionine beta-lyase, with chimeric mutants Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.4.1.13 K42A site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme Escherichia coli
4.4.1.13 additional information construction of 12 chimeric mutants of cystathionine gamma-synthase, EC 2.5.1.48, and cystathionine beta-lyase to probe the roles of two structurally distinct, about 25-residue segments situated in proximity to the amino and carboxy termini and located at the entrance of the active-site. The exchange of the targeted regions impairs the activity of the resulting enzymes, but does not produce a corresponding interchange of reaction specificity, catalytic efficiency of the native reactions is reduced by at least 95fold, and alpha,beta versus alpha,gamma-elimination specificity is not modified. The chimeric enzymes adopt a stable folded structure Escherichia coli
4.4.1.13 S32A site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme Escherichia coli
4.4.1.13 S33A site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.4.1.13 additional information
-
 additional information steady-state kinetics Escherichia coli
4.4.1.13 0.068
-
 L-cystathionine pH 8.5, 25°C, recombinant mutant S32A Escherichia coli
4.4.1.13 0.104
-
 L-cystathionine pH 8.5, 25°C, recombinant mutant S33A Escherichia coli
4.4.1.13 0.108
-
 L-cystathionine pH 8.5, 25°C, recombinant wild-type enzyme Escherichia coli
4.4.1.13 0.22
-
 L-cystathionine pH 8.5, 25°C, recombinant mutant K42A Escherichia coli
4.4.1.13 3.8
-
 L-cystathionine pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.4.1.13 L-cystathionine + H2O Escherichia coli
-
 L-homocysteine + pyruvate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.13 Escherichia coli P06721
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.13 L-cystathionine + H2O
-
 Escherichia coli L-homocysteine + pyruvate + NH3
-
 ?
4.4.1.13 O-acetyl-L-serine + H2O
-
 Escherichia coli acetate + pyruvate + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.4.1.13 CBL
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.4.1.13 25
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.4.1.13 4.24
-
 L-cystathionine pH 8.5, 25°C, recombinant mutant S33A Escherichia coli
4.4.1.13 6.78
-
 L-cystathionine pH 8.5, 25°C, recombinant mutant S32A Escherichia coli
4.4.1.13 6.8
-
 L-cystathionine pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL Escherichia coli
4.4.1.13 40.7
-
 L-cystathionine pH 8.5, 25°C, recombinant mutant K42A Escherichia coli
4.4.1.13 45.3
-
 L-cystathionine pH 8.5, 25°C, recombinant wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.4.1.13 8.5
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.4.1.13 pyridoxal 5'-phosphate
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
4.4.1.13 additional information cystathionine gamma-synthase, EC 2.5.1.48, and cystathionine beta-lyase sequence and structure comparison, both belonging to the gamma-subfamily of fold-type I, overview Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.4.1.13 1.76
-
 L-cystathionine pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL Escherichia coli
4.4.1.13 9.8
-
 L-cystathionine pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sN-eCBL Escherichia coli
4.4.1.13 41
-
 L-cystathionine pH 8.5, 25°C, recombinant mutant S33A Escherichia coli
4.4.1.13 99
-
 L-cystathionine pH 8.5, 25°C, recombinant mutant S32A Escherichia coli
4.4.1.13 190
-
 L-cystathionine pH 8.5, 25°C, recombinant mutant K42A Escherichia coli
4.4.1.13 420
-
 L-cystathionine pH 8.5, 25°C, recombinant wild-type enzyme Escherichia coli