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Literature summary for 4.4.1.13 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| K42A | site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme | Escherichia coli |
| 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 |
| S32A | site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme | Escherichia coli |
| S33A | site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics | Escherichia coli | |
| 0.068 | - |
L-cystathionine | pH 8.5, 25°C, recombinant mutant S32A | Escherichia coli |  |
| 0.104 | - |
L-cystathionine | pH 8.5, 25°C, recombinant mutant S33A | Escherichia coli | |
| 0.108 | - |
L-cystathionine | pH 8.5, 25°C, recombinant wild-type enzyme | Escherichia coli | |
| 0.22 | - |
L-cystathionine | pH 8.5, 25°C, recombinant mutant K42A | Escherichia coli | |
| 3.8 | - |
L-cystathionine | pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-cystathionine + H2O | Escherichia coli | - |
L-homocysteine + pyruvate + NH3 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P06721 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-cystathionine + H2O | - |
Escherichia coli | L-homocysteine + pyruvate + NH3 | - |
? | |
| O-acetyl-L-serine + H2O | - |
Escherichia coli | acetate + pyruvate + NH3 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CBL | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 4.24 | - |
L-cystathionine | pH 8.5, 25°C, recombinant mutant S33A | Escherichia coli | |
| 6.78 | - |
L-cystathionine | pH 8.5, 25°C, recombinant mutant S32A | Escherichia coli | |
| 6.8 | - |
L-cystathionine | pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL | Escherichia coli | |
| 40.7 | - |
L-cystathionine | pH 8.5, 25°C, recombinant mutant K42A | Escherichia coli | |
| 45.3 | - |
L-cystathionine | pH 8.5, 25°C, recombinant wild-type enzyme | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.76 | - |
L-cystathionine | pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL | Escherichia coli | |
| 9.8 | - |
L-cystathionine | pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sN-eCBL | Escherichia coli | |
| 41 | - |
L-cystathionine | pH 8.5, 25°C, recombinant mutant S33A | Escherichia coli | |
| 99 | - |
L-cystathionine | pH 8.5, 25°C, recombinant mutant S32A | Escherichia coli | |
| 190 | - |
L-cystathionine | pH 8.5, 25°C, recombinant mutant K42A | Escherichia coli | |
| 420 | - |
L-cystathionine | pH 8.5, 25°C, recombinant wild-type enzyme | Escherichia coli | |
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