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Literature summary extracted from
- Molecular characterization of mimosinase and cystathionine beta-lyase in the Mimosoideae subfamily member Mimosa pudica (2019), J. Plant Res., 132, 667-680 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.1.61 | DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Mimosa pudica |
| 4.4.1.13 | DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3) | Mimosa pudica |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.61 | 0.05 | - |
cystathionine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica |  |
| 3.5.1.61 | 1.95 | - |
mimosine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
| 4.4.1.13 | 2.4 | - |
cystathionine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.5.1.61 | additional information | the enzyme sequence contains a signal peptide | Mimosa pudica | - |
- |
| 4.4.1.13 | additional information | the enzyme sequence contains a signal peptide | Mimosa pudica | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.61 | cystathionine + H2O | Mimosa pudica | - |
homocysteine + pyruvate + NH3 | - |
? | |
| 3.5.1.61 | mimosine + H2O | Mimosa pudica | - |
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3 | - |
? | |
| 4.4.1.13 | cystathionine + H2O | Mimosa pudica | - |
homocysteine + pyruvate + NH3 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.61 | Mimosa pudica | U6BYK3 | - |
- |
| 4.4.1.13 | Mimosa pudica | A0A0M3VI47 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.5.1.61 | leaf | - |
Mimosa pudica | - |
| 3.5.1.61 | seedling | - |
Mimosa pudica | - |
| 4.4.1.13 | leaf | - |
Mimosa pudica | - |
| 4.4.1.13 | seedling | - |
Mimosa pudica | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.61 | cystathionine + H2O | - |
Mimosa pudica | homocysteine + pyruvate + NH3 | - |
? | |
| 3.5.1.61 | mimosine + H2O | - |
Mimosa pudica | 3-hydroxy-4-(1H)-pyridone + pyruvate + NH3 | - |
? | |
| 3.5.1.61 | additional information | substrate docking study. Cystathionine is a larger molecule than mimosine and consists of propyl (C3) and ethyl (C2) chains bound by a thioether linkage. The ethyl chain moiety and PLP of the complex interacts with Arg417, Lys255, Arg105', and Gly133 as is the case for mimosine | Mimosa pudica | ? | - |
? | |
| 4.4.1.13 | cystathionine + H2O | - |
Mimosa pudica | homocysteine + pyruvate + NH3 | - |
? | |
| 4.4.1.13 | additional information | substrate docking study. The largest attractive force that stabilizes the amino group of the ethyl chain moiety is contributed by Arg433. The negative charge of the carboxyl group in the ethyl chain is balanced by a hydrogen bond between it and amino group of Lys271. The propyl chain moiety of cystathionine is stabilized by the guanidium groups of two residues, Arg179 and Arg122'. Phosphate group of PLP forms two hydrogen bonds between hydroxy hydrogen of Ser268 and guanidium hydrogen of Arg122' | Mimosa pudica | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.61 | Mp mimosinase | - |
Mimosa pudica |
| 4.4.1.13 | CBL | - |
Mimosa pudica |
| 4.4.1.13 | Mp CBL | - |
Mimosa pudica |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.61 | 50 | - |
- |
Mimosa pudica |
| 4.4.1.13 | 50 | - |
- |
Mimosa pudica |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.61 | 70 | - |
purified recombinant GST-tagged enzyme, pH 8.0, stable up to | Mimosa pudica |
| 4.4.1.13 | 70 | - |
purified recombinant GST-tagged enzyme, pH 8.0, stable up to | Mimosa pudica |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.61 | 310 | - |
cystathionine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
| 3.5.1.61 | 12180 | - |
mimosine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
| 4.4.1.13 | 21000 | - |
cystathionine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.61 | 8 | 9 | - |
Mimosa pudica |
| 4.4.1.13 | 8 | - |
- |
Mimosa pudica |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.61 | pyridoxal 5'-phosphate | dependent on | Mimosa pudica | |
| 4.4.1.13 | pyridoxal 5'-phosphate | dependent on | Mimosa pudica | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.5.1.61 | malfunction | mutational analysis of Mp mimosinase reveals that the disruption of a disulfide bond in the vicinity of the pyridoxal 5'-phosphate domain increases the enzyme's preference toward cystathionine | Mimosa pudica |
| 3.5.1.61 | metabolism | molecular relationship between mimosinase and cystathionine beta-lyase (CBL, UniProt ID A0A0M3VI47, EC 4.4.1.13). The recombinant Mp mimosinase degrades both mimosine and cystathionine with a much higher turnover number for mimosine compared with cystathionine, and Mp CBL utilizes only cystathionine as a substrate | Mimosa pudica |
| 3.5.1.61 | additional information | homology modeling and molecular dynamics simulations of Mp mimosinase suggest a closer coordination of the residues that interact with mimosine at the active site compared with cystathionine, indicating a more compact pocket size for mimosine degradation, substrate docking study. Active site structure | Mimosa pudica |
| 4.4.1.13 | metabolism | molecular relationship between cystathionine beta-lyase and mimosinase (UniProt ID U6BYK3, EC 3.5.1.61). The recombinant Mp mimosinase degrades both mimosine and cystathionine with a much higher turnover number for mimosine compared with cystathionine, and Mp CBL utilizes only cystathionine as a substrate | Mimosa pudica |
| 4.4.1.13 | additional information | homology modeling and molecular dynamics simulations of Mp CBL. Active site structure | Mimosa pudica |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.61 | 6200 | - |
cystathionine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
| 3.5.1.61 | 6246 | - |
mimosine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
| 4.4.1.13 | 8750 | - |
cystathionine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
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Release 2023.1 (January 2023)
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