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Literature summary extracted from

  • Peverelli, M.G.; Soares da Costa, T.P.; Kirby, N.; Perugini, M.A.
    Dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis (2016), J. Biol. Chem., 291, 9785-9795 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.20 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis
4.1.1.20 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Escherichia coli
4.1.1.20 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus anthracis
4.1.1.20 recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Vibrio cholerae serotype O1

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.20 N381A site-directed mutagenesis, the mutant shows impaired dimerization and is significantly attenuated in catalytic activity Vibrio cholerae serotype O1
4.1.1.20 R385A site-directed mutagenesis, the mutant shows impaired dimerization and is significantly attenuated in catalytic activity Vibrio cholerae serotype O1

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.20 additional information
-
 additional information Michaelis-Menten kinetics, recombinant enzyme Mycobacterium tuberculosis
4.1.1.20 additional information
-
 additional information Michaelis-Menten kinetics, recombinant enzyme Escherichia coli
4.1.1.20 additional information
-
 additional information Michaelis-Menten kinetics, recombinant enzyme Bacillus anthracis
4.1.1.20 additional information
-
 additional information Michaelis-Menten kinetics, recombinant enzyme Vibrio cholerae serotype O1
4.1.1.20 0.68
-
 meso-2,6-diaminoheptanedioate pH 8.0, 37°C, recombinant enzyme Bacillus anthracis
4.1.1.20 0.97
-
 meso-2,6-diaminoheptanedioate pH 8.0, 37°C, recombinant enzyme Escherichia coli
4.1.1.20 1.6
-
 meso-2,6-diaminoheptanedioate pH 8.0, 37°C, recombinant enzyme Mycobacterium tuberculosis
4.1.1.20 1.9
-
 meso-2,6-diaminoheptanedioate pH 8.0, 37°C, recombinant enzyme Vibrio cholerae serotype O1

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.20 83000
-
 analytical ultracentrifugation Bacillus anthracis
4.1.1.20 92000
-
 analytical ultracentrifugation Vibrio cholerae serotype O1
4.1.1.20 100000
-
 about, analytical ultracentrifugation Mycobacterium tuberculosis
4.1.1.20 100000
-
 about, analytical ultracentrifugation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.20 meso-2,6-Diaminoheptanedioate Mycobacterium tuberculosis
-
 L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate Escherichia coli
-
 L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate Bacillus anthracis
-
 L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate Vibrio cholerae serotype O1
-
 L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate Bacillus anthracis Sterne
-
 L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
 L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
 L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate Escherichia coli K-12 / MG1655
-
 L-Lysine + CO2
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.20 Bacillus anthracis A0A1S0QVH4
-
-
4.1.1.20 Bacillus anthracis Sterne A0A1S0QVH4
-
-
4.1.1.20 Escherichia coli P00861
-
-
4.1.1.20 Escherichia coli K-12 / MG1655 P00861
-
-
4.1.1.20 Mycobacterium tuberculosis P9WIU7
-
-
4.1.1.20 Mycobacterium tuberculosis ATCC 25618 / H37Rv P9WIU7
-
-
4.1.1.20 Vibrio cholerae serotype O1 Q9KVL7
-
-
4.1.1.20 Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961 Q9KVL7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.20 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis
4.1.1.20 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Escherichia coli
4.1.1.20 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Bacillus anthracis
4.1.1.20 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Vibrio cholerae serotype O1

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.20 meso-2,6-Diaminoheptanedioate
-
 Mycobacterium tuberculosis L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate
-
 Escherichia coli L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate
-
 Bacillus anthracis L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate
-
 Vibrio cholerae serotype O1 L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate
-
 Bacillus anthracis Sterne L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate
-
 Mycobacterium tuberculosis ATCC 25618 / H37Rv L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate
-
 Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961 L-Lysine + CO2
-
 ir
4.1.1.20 meso-2,6-Diaminoheptanedioate
-
 Escherichia coli K-12 / MG1655 L-Lysine + CO2
-
 ir
4.1.1.20 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 ?
-
 ?
4.1.1.20 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 ?
-
 ?
4.1.1.20 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 ?
-
 ?
4.1.1.20 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 ?
-
 ?
4.1.1.20 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 ?
-
 ?
4.1.1.20 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 ?
-
 ?
4.1.1.20 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 ?
-
 ?
4.1.1.20 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 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.20 dimer 2 * 50000, about, SDS-PAGE Mycobacterium tuberculosis
4.1.1.20 dimer 2 * 40000, about, SDS-PAGE Bacillus anthracis
4.1.1.20 dimer 2 * 47400, about, SDS-PAGE Escherichia coli
4.1.1.20 dimer 2 * 50000, wild-type enzyme, about, SDS-PAGE, 2 x 49000, recombinant mutants N381A and R385A, SDS-PAGE Vibrio cholerae serotype O1
4.1.1.20 More 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
4.1.1.20 More 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
4.1.1.20 More 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
4.1.1.20 More 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

EC Number Synonyms Comment Organism
4.1.1.20 Ba-DAPDC
-
 Bacillus anthracis
4.1.1.20 BAS1329
-
 Bacillus anthracis
4.1.1.20 DAPDC
-
 Mycobacterium tuberculosis
4.1.1.20 DAPDC
-
 Escherichia coli
4.1.1.20 DAPDC
-
 Bacillus anthracis
4.1.1.20 DAPDC
-
 Vibrio cholerae serotype O1
4.1.1.20 diaminopimelate decarboxylase
-
 Mycobacterium tuberculosis
4.1.1.20 diaminopimelate decarboxylase
-
 Escherichia coli
4.1.1.20 diaminopimelate decarboxylase
-
 Bacillus anthracis
4.1.1.20 diaminopimelate decarboxylase
-
 Vibrio cholerae serotype O1
4.1.1.20 Ec-DAPDC
-
 Escherichia coli
4.1.1.20 LysA
-
 Mycobacterium tuberculosis
4.1.1.20 LysA
-
 Escherichia coli
4.1.1.20 LysA
-
 Bacillus anthracis
4.1.1.20 LysA
-
 Vibrio cholerae serotype O1
4.1.1.20 Mt-DAPDC
-
 Mycobacterium tuberculosis
4.1.1.20 Vc-DAPDC
-
 Vibrio cholerae serotype O1

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.20 37
-
 assay at Mycobacterium tuberculosis
4.1.1.20 37
-
 assay at Escherichia coli
4.1.1.20 37
-
 assay at Bacillus anthracis
4.1.1.20 37
-
 assay at Vibrio cholerae serotype O1

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.20 2 8 meso-2,6-diaminoheptanedioate pH 8.0, 37°C, recombinant enzyme Mycobacterium tuberculosis
4.1.1.20 22
-
 meso-2,6-diaminoheptanedioate pH 8.0, 37°C, recombinant enzyme Vibrio cholerae serotype O1
4.1.1.20 55
-
 meso-2,6-diaminoheptanedioate pH 8.0, 37°C, recombinant enzyme Escherichia coli
4.1.1.20 58
-
 meso-2,6-diaminoheptanedioate pH 8.0, 37°C, recombinant enzyme Bacillus anthracis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.20 8
-
 assay at Mycobacterium tuberculosis
4.1.1.20 8
-
 assay at Escherichia coli
4.1.1.20 8
-
 assay at Bacillus anthracis
4.1.1.20 8
-
 assay at Vibrio cholerae serotype O1

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.20 pyridoxal 5'-phosphate
-
 Mycobacterium tuberculosis
4.1.1.20 pyridoxal 5'-phosphate
-
 Escherichia coli
4.1.1.20 pyridoxal 5'-phosphate
-
 Bacillus anthracis
4.1.1.20 pyridoxal 5'-phosphate
-
 Vibrio cholerae serotype O1

General Information

EC Number General Information Comment Organism
4.1.1.20 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
4.1.1.20 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
4.1.1.20 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
4.1.1.20 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
4.1.1.20 additional information dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis Mycobacterium tuberculosis
4.1.1.20 additional information dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis Escherichia coli
4.1.1.20 additional information dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis Bacillus anthracis
4.1.1.20 additional information dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis Vibrio cholerae serotype O1
4.1.1.20 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
4.1.1.20 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
4.1.1.20 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
4.1.1.20 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