BRENDA - Enzyme Database show

Comparison of untagged and his-tagged dihydrodipicolinate synthase from the enteric pathogen Vibrio cholerae

Gupta, R.; Soares da Costa, T.P.; Faou, P.; Dogovski, C.; Perugini, M.A.; Protein Expr. Purif. 145, 85-93 (2018)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
4.3.3.7
drug development
the enzyme is an anti-cholera target
Vibrio cholerae
4.3.3.7
pharmacology
the enzyme is an anti-cholera target
Vibrio cholerae
Cloned(Commentary)
EC Number
Commentary
Organism
4.3.3.7
-
Vibrio cholerae
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.08
-
L-aspartate-4-semialdehyde
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
0.09
-
L-aspartate-4-semialdehyde
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
4.3.3.7
0.14
-
pyruvate
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
0.15
-
pyruvate
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.3.3.7
63000
-
recombinant untagged recombinant enzyme
Vibrio cholerae
4.3.3.7
68000
-
recombinant His-tagged recombinant enzyme
Vibrio cholerae
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
pyruvate + L-aspartate-4-semialdehyde
Vibrio cholerae
the enzyme catalyzes the first committed step in the diaminopimelate pathway
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
?
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
Vibrio cholerae O395
the enzyme catalyzes the first committed step in the diaminopimelate pathway
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
Vibrio cholerae
A5F699
-
-
4.3.3.7
Vibrio cholerae O395
A5F699
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.3.3.7
recombinant untagged and His-tagged enzymes
Vibrio cholerae
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.3.3.7
75.6
-
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
112
-
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
-
749225
Vibrio cholerae
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
the enzyme catalyzes the first committed step in the diaminopimelate pathway
749225
Vibrio cholerae
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
-
749225
Vibrio cholerae O395
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
the enzyme catalyzes the first committed step in the diaminopimelate pathway
749225
Vibrio cholerae O395
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
4.3.3.7
dimer
2 * 31000, SDS-PAGE, recombinant untagged recombinant enzyme; 2 * 33000, SDS-PAGE, recombinant His-tagged recombinant enzyme
Vibrio cholerae
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.3.3.7
34
-
L-aspartate-4-semialdehyde
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
34
-
pyruvate
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
46
-
L-aspartate-4-semialdehyde
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
4.3.3.7
46
-
pyruvate
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
Application (protein specific)
EC Number
Application
Commentary
Organism
4.3.3.7
drug development
the enzyme is an anti-cholera target
Vibrio cholerae
4.3.3.7
pharmacology
the enzyme is an anti-cholera target
Vibrio cholerae
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
4.3.3.7
-
Vibrio cholerae
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.08
-
L-aspartate-4-semialdehyde
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
0.09
-
L-aspartate-4-semialdehyde
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
4.3.3.7
0.14
-
pyruvate
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
0.15
-
pyruvate
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.3.3.7
63000
-
recombinant untagged recombinant enzyme
Vibrio cholerae
4.3.3.7
68000
-
recombinant His-tagged recombinant enzyme
Vibrio cholerae
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
pyruvate + L-aspartate-4-semialdehyde
Vibrio cholerae
the enzyme catalyzes the first committed step in the diaminopimelate pathway
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
?
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
Vibrio cholerae O395
the enzyme catalyzes the first committed step in the diaminopimelate pathway
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.3.3.7
recombinant untagged and His-tagged enzymes
Vibrio cholerae
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.3.3.7
75.6
-
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
112
-
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
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
pyruvate + L-aspartate-4-semialdehyde
-
749225
Vibrio cholerae
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
the enzyme catalyzes the first committed step in the diaminopimelate pathway
749225
Vibrio cholerae
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
-
749225
Vibrio cholerae O395
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
the enzyme catalyzes the first committed step in the diaminopimelate pathway
749225
Vibrio cholerae O395
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.3.3.7
dimer
2 * 31000, SDS-PAGE, recombinant untagged recombinant enzyme; 2 * 33000, SDS-PAGE, recombinant His-tagged recombinant enzyme
Vibrio cholerae
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.3.3.7
34
-
L-aspartate-4-semialdehyde
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
34
-
pyruvate
pH 8.0, 30°C, untagged enzyme
Vibrio cholerae
4.3.3.7
46
-
L-aspartate-4-semialdehyde
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
4.3.3.7
46
-
pyruvate
pH 8.0, 30°C, His-tagged enzyme
Vibrio cholerae
General Information
EC Number
General Information
Commentary
Organism
4.3.3.7
metabolism
the enzyme catalyzes the first committed step in the diaminopimelate pathway
Vibrio cholerae
General Information (protein specific)
EC Number
General Information
Commentary
Organism
4.3.3.7
metabolism
the enzyme catalyzes the first committed step in the diaminopimelate pathway
Vibrio cholerae