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Literature summary for 3.5.1.61 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)
| Cloned (Comment) | Organism |
|---|---|
| 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 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.05 | - |
cystathionine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica |  |
| 1.95 | - |
mimosine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | the enzyme sequence contains a signal peptide | Mimosa pudica | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cystathionine + H2O | Mimosa pudica | - |
homocysteine + pyruvate + NH3 | - |
? | |
| mimosine + H2O | Mimosa pudica | - |
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mimosa pudica | U6BYK3 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Mimosa pudica | - |
| seedling | - |
Mimosa pudica | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cystathionine + H2O | - |
Mimosa pudica | homocysteine + pyruvate + NH3 | - |
? | |
| mimosine + H2O | - |
Mimosa pudica | 3-hydroxy-4-(1H)-pyridone + pyruvate + NH3 | - |
? | |
| 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 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Mp mimosinase | - |
Mimosa pudica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Mimosa pudica |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
purified recombinant GST-tagged enzyme, pH 8.0, stable up to | Mimosa pudica |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 310 | - |
cystathionine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
| 12180 | - |
mimosine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 9 | - |
Mimosa pudica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | dependent on | Mimosa pudica | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 6200 | - |
cystathionine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
| 6246 | - |
mimosine | pH 8.5, 37°C, recombinant enzyme | Mimosa pudica | |
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