BRENDA - Enzyme Database show

Identification of the bona fide DHDPS from a common plant pathogen

Atkinson, S.; Hor, L.; Dogovski, C.; Dobson, R.; Perugini, M.; Proteins 82, 1869-1883 (2014)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
4.3.3.7
drug development
the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents; the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents; the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents; the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents; the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents; the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents; the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents; the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents; the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents; the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents
Agrobacterium tumefaciens
Cloned(Commentary)
EC Number
Commentary
Organism
4.3.3.7
gene dapA10, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3); gene dapA1, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3); gene dapA2, sequence comparisons, expression of the His-tagged isozyme in Escherichia coli strain BL21(DE3); gene dapA3, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3); gene dapA4, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3); gene dapA5, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3); gene dapA6, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3); gene dapA7, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3); gene dapA8, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3); gene dapA9, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
Crystallization (Commentary)
EC Number
Crystallization
Organism
4.3.3.7
crystal structure analysis, PDB ID 2HMC, structure comparisons; crystal structure analysis, PDB ID 2R8Wm, structure comparisons; crystal structure analysis, PDB ID 3B4U, structure comparisons; crystal structure analysis, PDB IDs 4I7U, 4I7V, and 4I7W, resolution at 1.42-1.69 A, structure comparisons
Agrobacterium tumefaciens
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
(S)-aspartate-4-semialdehyde
substrate inhibition
Agrobacterium tumefaciens
4.3.3.7
(S)-lysine
allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition, allosteric site modeling; allosteric feedback inhibition, allosteric site modeling; allosteric feedback inhibition, allosteric site modeling; allosteric feedback inhibition, allosteric site modeling
Agrobacterium tumefaciens
4.3.3.7
pyruvate
substrate inhibition
Agrobacterium tumefaciens
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.16
0.32
(S)-aspartate-4-semialdehyde
pH and temperature not specified in the publication
Agrobacterium tumefaciens
4.3.3.7
0.31
0.44
pyruvate
pH and temperature not specified in the publication
Agrobacterium tumefaciens
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
Agrobacterium tumefaciens
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
?
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
Agrobacterium tumefaciens C58 / ATCC 33970
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
Agrobacterium tumefaciens
A9CFV4
dapA10; gene dapA10
-
4.3.3.7
Agrobacterium tumefaciens
A9CGZ4
dapA8; gene dapA8
-
4.3.3.7
Agrobacterium tumefaciens
A9CHR2
dapA5; gene dapA5
-
4.3.3.7
Agrobacterium tumefaciens
A9CL94
dapA2; genes dapA2
-
4.3.3.7
Agrobacterium tumefaciens
A9CL97
dapA3; gene dapA3
-
4.3.3.7
Agrobacterium tumefaciens
Q7CU96
dapA9; gene dapA9
-
4.3.3.7
Agrobacterium tumefaciens
Q7D0E8
dapA6; gene dapA6
-
4.3.3.7
Agrobacterium tumefaciens
Q7D313
dapA1; gene dapA1
-
4.3.3.7
Agrobacterium tumefaciens
Q7D3Z9
dapA4; gene dapA4
-
4.3.3.7
Agrobacterium tumefaciens
Q8UGL3
dapA7; gene dapA7
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
A9CFV4
dapA10; gene dapA10
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
A9CGZ4
dapA8; gene dapA8
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
A9CHR2
dapA5; gene dapA5
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
A9CL94
dapA2; genes dapA2
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
A9CL97
dapA3; gene dapA3
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
Q7CU96
dapA9; gene dapA9
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
Q7D0E8
dapA6; gene dapA6
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
Q7D313
dapA1; gene dapA1
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
Q7D3Z9
dapA4; gene dapA4
-
4.3.3.7
Agrobacterium tumefaciens C58 / ATCC 33970
Q8UGL3
dapA7; gene dapA7
-
Purification (Commentary)
EC Number
Commentary
Organism
4.3.3.7
recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography; recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography; recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography; recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography; recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography; recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography; recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography; recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography; recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography; recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
Agrobacterium tumefaciens
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
-
730915
Agrobacterium tumefaciens
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
?
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
bi-bi ping-pong substrate model
730915
Agrobacterium tumefaciens
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
?
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
-
730915
Agrobacterium tumefaciens C58 / ATCC 33970
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
?
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
bi-bi ping-pong substrate model
730915
Agrobacterium tumefaciens C58 / ATCC 33970
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
4.3.3.7
homotetramer
the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state; the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state; the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state; the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state; the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state; the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state; the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state; the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state; the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state; the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state
Agrobacterium tumefaciens
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.3.3.7
0.15
-
(S)-aspartate-4-semialdehyde
pH and temperature not specified in the publication
Agrobacterium tumefaciens
4.3.3.7
0.19
0.57
pyruvate
pH and temperature not specified in the publication
Agrobacterium tumefaciens
Application (protein specific)
EC Number
Application
Commentary
Organism
4.3.3.7
drug development
the enzyme is a bona fide drug target for treatment of the Crown Gall disease on crops caused by Agrobacterium tumefaciens, rational design of pesticide agents
Agrobacterium tumefaciens
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
4.3.3.7
gene dapA1, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
4.3.3.7
gene dapA10, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
4.3.3.7
gene dapA2, sequence comparisons, expression of the His-tagged isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
4.3.3.7
gene dapA3, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
4.3.3.7
gene dapA4, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
4.3.3.7
gene dapA5, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
4.3.3.7
gene dapA6, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
4.3.3.7
gene dapA7, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
4.3.3.7
gene dapA8, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
4.3.3.7
gene dapA9, sequence comparisons, expression of the His-tagged enzyme isozyme in Escherichia coli strain BL21(DE3)
Agrobacterium tumefaciens
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.3.3.7
crystal structure analysis, PDB ID 2HMC, structure comparisons
Agrobacterium tumefaciens
4.3.3.7
crystal structure analysis, PDB ID 2R8Wm, structure comparisons
Agrobacterium tumefaciens
4.3.3.7
crystal structure analysis, PDB ID 3B4U, structure comparisons
Agrobacterium tumefaciens
4.3.3.7
crystal structure analysis, PDB IDs 4I7U, 4I7V, and 4I7W, resolution at 1.42-1.69 A, structure comparisons
Agrobacterium tumefaciens
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
(S)-aspartate-4-semialdehyde
substrate inhibition
Agrobacterium tumefaciens
4.3.3.7
(S)-lysine
allosteric feedback inhibition
Agrobacterium tumefaciens
4.3.3.7
(S)-lysine
allosteric feedback inhibition, allosteric site modeling
Agrobacterium tumefaciens
4.3.3.7
pyruvate
substrate inhibition
Agrobacterium tumefaciens
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.3.3.7
0.15
-
(S)-aspartate-4-semialdehyde
pH and temperature not specified in the publication
Agrobacterium tumefaciens
4.3.3.7
0.19
0.57
pyruvate
pH and temperature not specified in the publication
Agrobacterium tumefaciens
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.16
0.32
(S)-aspartate-4-semialdehyde
pH and temperature not specified in the publication
Agrobacterium tumefaciens
4.3.3.7
0.31
0.44
pyruvate
pH and temperature not specified in the publication
Agrobacterium tumefaciens
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
Agrobacterium tumefaciens
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
?
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
Agrobacterium tumefaciens C58 / ATCC 33970
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.3.3.7
recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
Agrobacterium tumefaciens
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
-
730915
Agrobacterium tumefaciens
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
?
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
bi-bi ping-pong substrate model
730915
Agrobacterium tumefaciens
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
?
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
-
730915
Agrobacterium tumefaciens C58 / ATCC 33970
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
?
4.3.3.7
(S)-aspartate-4-semialdehyde + pyruvate
bi-bi ping-pong substrate model
730915
Agrobacterium tumefaciens C58 / ATCC 33970
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.3.3.7
homotetramer
the enzyme adopts the canonical homotetrameric structure in both solution and the crystal state
Agrobacterium tumefaciens
General Information
EC Number
General Information
Commentary
Organism
4.3.3.7
metabolism
the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid; the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid; the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid; the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid; the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid; the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid; the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid; the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid; the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid; the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid
Agrobacterium tumefaciens
4.3.3.7
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent; the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent; the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent; the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent; the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent; the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent; the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent; the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent; the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent; the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
Agrobacterium tumefaciens
General Information (protein specific)
EC Number
General Information
Commentary
Organism
4.3.3.7
metabolism
the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid
Agrobacterium tumefaciens
4.3.3.7
additional information
the catalytic triad, consisting of Tyr133, Thr44, and Tyr107, acts as a proton relay to transfer protons to and from the active site via a water-filled channel leading to bulk solvent
Agrobacterium tumefaciens