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) | Mycobacterium tuberculosis |
gene lysA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Escherichia coli |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
meso-2,6-Diaminoheptanedioate | Mycobacterium tuberculosis | - |
L-Lysine + CO2 | - |
? | |
meso-2,6-Diaminoheptanedioate | Escherichia coli | - |
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 | 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 (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 | Mycobacterium tuberculosis |
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and gel filtration | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
meso-2,6-Diaminoheptanedioate | - |
Mycobacterium tuberculosis | L-Lysine + CO2 | - |
? | |
meso-2,6-Diaminoheptanedioate | - |
Escherichia coli | 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 | 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 | 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 | 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 | Comment | Organism |
---|---|---|
BAS1329 | - |
Bacillus anthracis |
DAPDC | - |
Mycobacterium tuberculosis |
DAPDC | - |
Escherichia coli |
DAPDC | - |
Bacillus anthracis |
diaminopimelate decarboxylase | - |
Mycobacterium tuberculosis |
diaminopimelate decarboxylase | - |
Escherichia coli |
diaminopimelate decarboxylase | - |
Bacillus anthracis |
LysA | - |
Mycobacterium tuberculosis |
LysA | - |
Escherichia coli |
LysA | - |
Bacillus anthracis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mycobacterium tuberculosis |
37 | - |
assay at | Escherichia coli |
37 | - |
assay at | Bacillus anthracis |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Mycobacterium tuberculosis |
8 | - |
assay at | Escherichia coli |
8 | - |
assay at | Bacillus anthracis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Mycobacterium tuberculosis | |
pyridoxal 5'-phosphate | - |
Escherichia coli | |
pyridoxal 5'-phosphate | - |
Bacillus anthracis |
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 | 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 | 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 | Bacillus anthracis |