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Literature summary for 4.1.1.20 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)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis
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) Bacillus anthracis
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 Mycobacterium tuberculosis
additional information
-
additional information Michaelis-Menten kinetics, recombinant enzyme Escherichia coli
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 Mycobacterium tuberculosis
100000
-
about, analytical ultracentrifugation Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
meso-2,6-Diaminoheptanedioate Mycobacterium tuberculosis
-
L-Lysine + CO2
-
ir
meso-2,6-Diaminoheptanedioate Escherichia coli
-
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 Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
L-Lysine + CO2
-
ir
meso-2,6-Diaminoheptanedioate Escherichia coli K-12 / MG1655
-
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) Mycobacterium tuberculosis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Escherichia coli
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Bacillus anthracis
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
-
Mycobacterium tuberculosis L-Lysine + CO2
-
ir
meso-2,6-Diaminoheptanedioate
-
Escherichia coli 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
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961 L-Lysine + CO2
-
ir
meso-2,6-Diaminoheptanedioate
-
Escherichia coli K-12 / MG1655 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 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 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 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 Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961 ?
-
?
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

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

Synonyms Comment Organism
Ba-DAPDC
-
Bacillus anthracis
BAS1329
-
Bacillus anthracis
DAPDC
-
Mycobacterium tuberculosis
DAPDC
-
Escherichia coli
DAPDC
-
Bacillus anthracis
DAPDC
-
Vibrio cholerae serotype O1
diaminopimelate decarboxylase
-
Mycobacterium tuberculosis
diaminopimelate decarboxylase
-
Escherichia coli
diaminopimelate decarboxylase
-
Bacillus anthracis
diaminopimelate decarboxylase
-
Vibrio cholerae serotype O1
Ec-DAPDC
-
Escherichia coli
LysA
-
Mycobacterium tuberculosis
LysA
-
Escherichia coli
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 Mycobacterium tuberculosis
37
-
assay at Escherichia coli
37
-
assay at Bacillus anthracis
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 Mycobacterium tuberculosis
8
-
assay at Escherichia coli
8
-
assay at Bacillus anthracis
8
-
assay at Vibrio cholerae serotype O1

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Mycobacterium tuberculosis
pyridoxal 5'-phosphate
-
Escherichia coli
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 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 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 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 Mycobacterium tuberculosis
additional information dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis Escherichia coli
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 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 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 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