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Literature summary for 4.1.1.20 extracted from
- Dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis (2016), J. Biol. Chem., 291, 9785-9795 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus anthracis |
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Escherichia coli |
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Mycobacterium tuberculosis |
| recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Vibrio cholerae serotype O1 |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| N381A | site-directed mutagenesis, the mutant shows impaired dimerization and is significantly attenuated in catalytic activity | Vibrio cholerae serotype O1 |
| R385A | site-directed mutagenesis, the mutant shows impaired dimerization and is significantly attenuated in catalytic activity | Vibrio cholerae serotype O1 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics, recombinant enzyme | Escherichia coli | |
| additional information | - |
additional information | Michaelis-Menten kinetics, recombinant enzyme | Mycobacterium tuberculosis | |
| additional information | - |
additional information | Michaelis-Menten kinetics, recombinant enzyme | Bacillus anthracis | |
| additional information | - |
additional information | Michaelis-Menten kinetics, recombinant enzyme | Vibrio cholerae serotype O1 | |
| 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 | |
| 1.6 | - |
meso-2,6-diaminoheptanedioate | pH 8.0, 37°C, recombinant enzyme | Mycobacterium tuberculosis | |
| 1.9 | - |
meso-2,6-diaminoheptanedioate | pH 8.0, 37°C, recombinant enzyme | Vibrio cholerae serotype O1 | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 83000 | - |
analytical ultracentrifugation | Bacillus anthracis |
| 92000 | - |
analytical ultracentrifugation | Vibrio cholerae serotype O1 |
| 100000 | - |
about, analytical ultracentrifugation | Escherichia coli |
| 100000 | - |
about, analytical ultracentrifugation | 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 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | Mycobacterium tuberculosis | - |
L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | Bacillus anthracis | - |
L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | Vibrio cholerae serotype O1 | - |
L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | Bacillus anthracis Sterne | - |
L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | Mycobacterium tuberculosis ATCC 25618 / H37Rv | - |
L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | Escherichia coli K-12 / MG1655 | - |
L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961 | - |
L-Lysine + CO2 | - |
ir | |
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 | - |
- |
| Vibrio cholerae serotype O1 | Q9KVL7 | - |
- |
| Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961 | Q9KVL7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) | Bacillus anthracis |
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) | Escherichia coli |
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) | Mycobacterium tuberculosis |
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) | Vibrio cholerae serotype O1 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| meso-2,6-Diaminoheptanedioate | - |
Escherichia coli | L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | - |
Mycobacterium tuberculosis | L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | - |
Bacillus anthracis | L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | - |
Vibrio cholerae serotype O1 | L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | - |
Bacillus anthracis Sterne | L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | - |
Mycobacterium tuberculosis ATCC 25618 / H37Rv | L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | - |
Escherichia coli K-12 / MG1655 | L-Lysine + CO2 | - |
ir | |
| meso-2,6-Diaminoheptanedioate | - |
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961 | L-Lysine + CO2 | - |
ir | |
| additional information | usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Escherichia coli | ? | - |
? | |
| additional information | usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Mycobacterium tuberculosis | ? | - |
? | |
| additional information | usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Bacillus anthracis | ? | - |
? | |
| additional information | usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Vibrio cholerae serotype O1 | ? | - |
? | |
| additional information | usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Bacillus anthracis Sterne | ? | - |
? | |
| additional information | usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Mycobacterium tuberculosis ATCC 25618 / H37Rv | ? | - |
? | |
| additional information | usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Escherichia coli K-12 / MG1655 | ? | - |
? | |
| additional information | usage of a quantitative assay for measuring DAPDC catalytic activity with saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae as the coupling enzyme, SDH has optimal activity at 37°C, pH 8.0, and in Tris buffer | Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 47400, about, SDS-PAGE | Escherichia coli |
| dimer | 2 * 50000, about, SDS-PAGE | Mycobacterium tuberculosis |
| dimer | 2 * 40000, about, SDS-PAGE | Bacillus anthracis |
| dimer | 2 * 50000, wild-type enzyme, about, SDS-PAGE, 2 x 49000, recombinant mutants N381A and R385A, SDS-PAGE | Vibrio cholerae serotype O1 |
| additional information | dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis, secondary and quaternary structure analysis of soluble recombinant enzyme, analysis by SDS-PAGE, fluorescence-detected analytical ultracentrifugation, mass spectrometry, and circular dichroism spectroscopy, detailed overview | Escherichia coli |
| additional information | dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis, secondary and quaternary structure analysis of soluble recombinant enzyme, analysis by SDS-PAGE, fluorescence-detected analytical ultracentrifugation, mass spectrometry, and circular dichroism spectroscopy, detailed overview | Mycobacterium tuberculosis |
| additional information | dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis, secondary and quaternary structure analysis of soluble recombinant enzyme, analysis by SDS-PAGE, fluorescence-detected analytical ultracentrifugation, mass spectrometry, and circular dichroism spectroscopy, detailed overview | Bacillus anthracis |
| additional information | dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis, secondary and quaternary structure analysis of soluble recombinant enzyme, analysis by SDS-PAGE, fluorescence-detected analytical ultracentrifugation, mass spectrometry, and circular dichroism spectroscopy, detailed overview | Vibrio cholerae serotype O1 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Ba-DAPDC | - |
Bacillus anthracis |
| BAS1329 | - |
Bacillus anthracis |
| DAPDC | - |
Escherichia coli |
| DAPDC | - |
Mycobacterium tuberculosis |
| DAPDC | - |
Bacillus anthracis |
| DAPDC | - |
Vibrio cholerae serotype O1 |
| diaminopimelate decarboxylase | - |
Escherichia coli |
| diaminopimelate decarboxylase | - |
Mycobacterium tuberculosis |
| diaminopimelate decarboxylase | - |
Bacillus anthracis |
| diaminopimelate decarboxylase | - |
Vibrio cholerae serotype O1 |
| Ec-DAPDC | - |
Escherichia coli |
| LysA | - |
Escherichia coli |
| LysA | - |
Mycobacterium tuberculosis |
| LysA | - |
Bacillus anthracis |
| LysA | - |
Vibrio cholerae serotype O1 |
| Mt-DAPDC | - |
Mycobacterium tuberculosis |
| Vc-DAPDC | - |
Vibrio cholerae serotype O1 |
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 |
| 37 | - |
assay at | Vibrio cholerae serotype O1 |
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 | |
| 22 | - |
meso-2,6-diaminoheptanedioate | pH 8.0, 37°C, recombinant enzyme | Vibrio cholerae serotype O1 | |
| 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 |
| 8 | - |
assay at | Vibrio cholerae serotype O1 |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Escherichia coli | |
| pyridoxal 5'-phosphate | - |
Mycobacterium tuberculosis | |
| pyridoxal 5'-phosphate | - |
Bacillus anthracis | |
| pyridoxal 5'-phosphate | - |
Vibrio cholerae serotype O1 | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme catalyzes the irreversible and stereospecific decarboxylation of meso-diaminopimelate (meso-DAP) in the final step of the diaminopimelate (DAP) biosynthesis pathway | Escherichia coli |
| metabolism | the enzyme catalyzes the irreversible and stereospecific decarboxylation of meso-diaminopimelate (meso-DAP) in the final step of the diaminopimelate (DAP) biosynthesis pathway | Mycobacterium tuberculosis |
| metabolism | the enzyme catalyzes the irreversible and stereospecific decarboxylation of meso-diaminopimelate (meso-DAP) in the final step of the diaminopimelate (DAP) biosynthesis pathway | Bacillus anthracis |
| metabolism | the enzyme catalyzes the irreversible and stereospecific decarboxylation of meso-diaminopimelate (meso-DAP) in the final step of the diaminopimelate (DAP) biosynthesis pathway | Vibrio cholerae serotype O1 |
| additional information | dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis | Escherichia coli |
| additional information | dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis | Mycobacterium tuberculosis |
| additional information | dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis | Bacillus anthracis |
| additional information | dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis | Vibrio cholerae serotype O1 |
| physiological function | the product of the reaction, L-lysine, is an important building block for the biosynthesis of the peptidoglycan cell wall, housekeeping proteins, and virulence factors of bacteria | Escherichia coli |
| physiological function | the product of the reaction, L-lysine, is an important building block for the biosynthesis of the peptidoglycan cell wall, housekeeping proteins, and virulence factors of bacteria | Mycobacterium tuberculosis |
| physiological function | the product of the reaction, L-lysine, is an important building block for the biosynthesis of the peptidoglycan cell wall, housekeeping proteins, and virulence factors of bacteria | Bacillus anthracis |
| physiological function | the product of the reaction, L-lysine, is an important building block for the biosynthesis of the peptidoglycan cell wall, housekeeping proteins, and virulence factors of bacteria | Vibrio cholerae serotype O1 |
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