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Literature summary for 4.1.1.20 extracted from
- An optimized coupled assay for quantifying diaminopimelate decarboxylase activity (2015), Biochimie, 115, 78-85 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene lysA, recombinant enzyme expression in Escherichia coli strain BL21(DE3) | Bacillus anthracis |
| gene lysA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Escherichia coli |
| gene lysA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Mycobacterium tuberculosis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.68 | - |
meso-2,6-diaminoheptanedioate | pH 8.0, 37°C, recombinant enzyme | Bacillus anthracis |  |
| 0.97 | - |
meso-2,6-diaminoheptanedioate | pH 8.0, 37°C, recombinant enzyme | Escherichia coli | |
| 1.62 | - |
meso-2,6-diaminoheptanedioate | pH 8.0, 37°C, recombinant enzyme | Mycobacterium tuberculosis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| meso-2,6-Diaminoheptanedioate | Escherichia coli | - |
L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | Mycobacterium tuberculosis | - |
L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | Bacillus anthracis | - |
L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | Bacillus anthracis Sterne | - |
L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | Mycobacterium tuberculosis ATCC 25618 / H37Rv | - |
L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | Escherichia coli K-12 / MG1655 | - |
L-Lysine + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus anthracis | A0A1S0QVH4 | - |
- |
| Bacillus anthracis Sterne | A0A1S0QVH4 | - |
- |
| Escherichia coli | P00861 | - |
- |
| Escherichia coli K-12 / MG1655 | P00861 | - |
- |
| Mycobacterium tuberculosis | P9WIU7 | - |
- |
| Mycobacterium tuberculosis ATCC 25618 / H37Rv | P9WIU7 | - |
- |
| no activity in Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, and gel filtration | Bacillus anthracis |
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and gel filtration | Escherichia coli |
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and gel filtration | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| meso-2,6-Diaminoheptanedioate | - |
Escherichia coli | L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | - |
Mycobacterium tuberculosis | L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | - |
Bacillus anthracis | L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | - |
Bacillus anthracis Sterne | L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | - |
Mycobacterium tuberculosis ATCC 25618 / H37Rv | L-Lysine + CO2 | - |
? | |
| meso-2,6-Diaminoheptanedioate | - |
Escherichia coli K-12 / MG1655 | L-Lysine + CO2 | - |
? | |
| additional information | optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Escherichia coli | ? | - |
? | |
| additional information | optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Mycobacterium tuberculosis | ? | - |
? | |
| additional information | optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Bacillus anthracis | ? | - |
? | |
| additional information | optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Bacillus anthracis Sterne | ? | - |
? | |
| additional information | optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Mycobacterium tuberculosis ATCC 25618 / H37Rv | ? | - |
? | |
| additional information | optimization of a simple quantitative assay for measuring DAPDC catalytic activity using saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, method, overview. SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Escherichia coli K-12 / MG1655 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BAS1329 | - |
Bacillus anthracis |
| DAPDC | - |
Escherichia coli |
| DAPDC | - |
Mycobacterium tuberculosis |
| DAPDC | - |
Bacillus anthracis |
| diaminopimelate decarboxylase | - |
Escherichia coli |
| diaminopimelate decarboxylase | - |
Mycobacterium tuberculosis |
| diaminopimelate decarboxylase | - |
Bacillus anthracis |
| LysA | - |
Escherichia coli |
| LysA | - |
Mycobacterium tuberculosis |
| LysA | - |
Bacillus anthracis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Bacillus anthracis |
| 37 | - |
assay at | Escherichia coli |
| 37 | - |
assay at | Mycobacterium tuberculosis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2 | 8 | meso-2,6-diaminoheptanedioate | pH 8.0, 37°C, recombinant enzyme | Mycobacterium tuberculosis | |
| 55 | - |
meso-2,6-diaminoheptanedioate | pH 8.0, 37°C, recombinant enzyme | Escherichia coli | |
| 58 | - |
meso-2,6-diaminoheptanedioate | pH 8.0, 37°C, recombinant enzyme | Bacillus anthracis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Escherichia coli |
| 8 | - |
assay at | Mycobacterium tuberculosis |
| 8 | - |
assay at | Bacillus anthracis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Escherichia coli | |
| pyridoxal 5'-phosphate | - |
Mycobacterium tuberculosis | |
| pyridoxal 5'-phosphate | - |
Bacillus anthracis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | diaminopimelate decarboxylase (DAPDC) catalyzes the conversion of meso-2,6-diaminopimelate to lysine and carbon dioxide in the final step of the diaminopimelate (DAP) pathway | Escherichia coli |
| metabolism | diaminopimelate decarboxylase (DAPDC) catalyzes the conversion of meso-2,6-diaminopimelate to lysine and carbon dioxide in the final step of the diaminopimelate (DAP) pathway | Mycobacterium tuberculosis |
| metabolism | diaminopimelate decarboxylase (DAPDC) catalyzes the conversion of meso-2,6-diaminopimelate to lysine and carbon dioxide in the final step of the diaminopimelate (DAP) pathway | Bacillus anthracis |
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