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Literature summary for 4.1.1.18 extracted from
- Characterization of a whole-cell biotransformation using a constitutive lysine decarboxylase from Escherichia coli for the high-level production of cadaverine from industrial grade L-lysine (2018), Appl. Biochem. Biotechnol., 185, 909-924 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | CadA is the conventional cadaverine producer | Escherichia coli |
| synthesis | the enzyme EcLdcC can be used for whole-cell biotransformation (a whole-cell biocatalyst) using a constitutive lysine decarboxylase from Escherichia coli for the high-level production of cadaverine from industrial grade L-lysine. It is more effective in comparison to EcCadA. Cadaverine is used for synthesis of bio-polyamides | Escherichia coli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene cadA, recombinant induced expression of lysine decarboxylase in Escherichia coli strain BL21(DE3) for the high-level production of cadaverine from industrial grade L-lysine | Escherichia coli |
| gene ldcC, recombinant constitutive expression of lysine decarboxylase in Escherichia coli strain BL21(DE3) for the high-level production of cadaverine from industrial grade L-lysine | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | recombinant Escherichia coli-overexpressing CadA produces cadaverine from crude L-lysine solution. Constitutive lysine decarboxylase EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing the inducible lysine carboxylase CadA, the conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine | Escherichia coli |
| additional information | recombinant Escherichia coli-overexpressing LdcC (EcLdcC) produces cadaverine from crude L-lysine solution. EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing an inducible lysine carboxylase (CadA), a conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine. Optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| L-lysine | substrate inhibition at high concentrations | Escherichia coli |  |
| additional information | enzyme LdcC shows no or poor substrate inhibition by L-lysine | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | - |
Escherichia coli | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-lysine | Escherichia coli | - |
cadaverine + CO2 | - |
? | |
| L-lysine | Escherichia coli K-12 / MG1655 | - |
cadaverine + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A9H3 | - |
- |
| Escherichia coli | P52095 | - |
- |
| Escherichia coli K-12 / MG1655 | P0A9H3 | - |
- |
| Escherichia coli K-12 / MG1655 | P52095 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-lysine | - |
Escherichia coli | cadaverine + CO2 | - |
? | |
| L-lysine | - |
Escherichia coli K-12 / MG1655 | cadaverine + CO2 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CadA | - |
Escherichia coli |
| constitutive lysine decarboxylase | - |
Escherichia coli |
| inducible lysine decarboxylase | - |
Escherichia coli |
| LDC | - |
Escherichia coli |
| ldcC | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
in vivo assay at | Escherichia coli |
| 52 | - |
recombinant enzyme | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6 | - |
Escherichia coli |
| 6 | 7 | in vitro | Escherichia coli |
| 6 | - |
in vivo | Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
CadA is rapidly inactivated as the pH increases during the decarboxylation of lysine because it has an acidic optimum pH 5.0-6.0 | Escherichia coli |
| 4 | 10 | activity range | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Escherichia coli | |
| pyridoxal 5'-phosphate | best at 0.01 mM | Escherichia coli | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Escherichia coli | pH-inducible CadA | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview | Escherichia coli |
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