BRENDA - Enzyme Database show

Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization

Laber, B.; Gomis-Rueth, F.X.; Romao, M.J.; Huber, R.; Biochem. J. 268, 691-695 (1992)
No PubMed abstract available

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.3.3.7
-
Escherichia coli
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
3-Bromopyruvate
-
Escherichia coli
4.3.3.7
dipicolinic acid
1.2 mM, 50% inhibition
Escherichia coli
4.3.3.7
L-lysine
1 mM, 50% inhibition
Escherichia coli
4.3.3.7
S-(2-aminoethyl)-L-cysteine
4.6 mM, 50% inhibition
Escherichia coli
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.55
-
DL-aspartate-4-semialdehyde
-
Escherichia coli
4.3.3.7
0.57
-
pyruvate
-
Escherichia coli
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.3.3.7
32000
-
4 * 32000, Lys161 is the active site, SDS-PAGE
Escherichia coli
4.3.3.7
112000
-
gel filtration
Escherichia coli
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
L-aspartate-4-semialdehyde + pyruvate
Escherichia coli
synthesis of the precursor of dipicolinic acid which plays a key role in bacterial sporulation process
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
Escherichia coli
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.3.3.7
-
Escherichia coli
Reaction
EC Number
Reaction
Commentary
Organism
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
pyruvate binds to the enzyme first by forming a Schiff base with the epsilon-amino group of Lys161. After release of the first water molecule L-aspartate-4-semialdehyde binds to the active site and the condensation reaction to form 2,3-dihydrodipicolinate takes place
Escherichia coli
Storage Stability
EC Number
Storage Stability
Organism
4.3.3.7
-20°C, addition of glycerol, several months, no loss of activity
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
L-aspartate-4-semialdehyde + pyruvate
-
33912
Escherichia coli
dihydrodipicolinate + H2O
-
33912
Escherichia coli
?
4.3.3.7
L-aspartate-4-semialdehyde + pyruvate
synthesis of the precursor of dipicolinic acid which plays a key role in bacterial sporulation process
33912
Escherichia coli
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
4.3.3.7
tetramer
4 * 32000, Lys161 is the active site, SDS-PAGE
Escherichia coli
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.3.3.7
1
-
L-lysine
-
Escherichia coli
4.3.3.7
1.2
-
dipicolinic acid
-
Escherichia coli
4.3.3.7
4.6
-
S-(2-aminoethyl)-L-cysteine
-
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.3.3.7
-
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
3-Bromopyruvate
-
Escherichia coli
4.3.3.7
dipicolinic acid
1.2 mM, 50% inhibition
Escherichia coli
4.3.3.7
L-lysine
1 mM, 50% inhibition
Escherichia coli
4.3.3.7
S-(2-aminoethyl)-L-cysteine
4.6 mM, 50% inhibition
Escherichia coli
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.3.3.7
1
-
L-lysine
-
Escherichia coli
4.3.3.7
1.2
-
dipicolinic acid
-
Escherichia coli
4.3.3.7
4.6
-
S-(2-aminoethyl)-L-cysteine
-
Escherichia coli
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.55
-
DL-aspartate-4-semialdehyde
-
Escherichia coli
4.3.3.7
0.57
-
pyruvate
-
Escherichia coli
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.3.3.7
32000
-
4 * 32000, Lys161 is the active site, SDS-PAGE
Escherichia coli
4.3.3.7
112000
-
gel filtration
Escherichia coli
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
L-aspartate-4-semialdehyde + pyruvate
Escherichia coli
synthesis of the precursor of dipicolinic acid which plays a key role in bacterial sporulation process
?
-
-
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.3.3.7
-
Escherichia coli
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
4.3.3.7
-20°C, addition of glycerol, several months, no loss of activity
Escherichia coli
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
L-aspartate-4-semialdehyde + pyruvate
-
33912
Escherichia coli
dihydrodipicolinate + H2O
-
33912
Escherichia coli
?
4.3.3.7
L-aspartate-4-semialdehyde + pyruvate
synthesis of the precursor of dipicolinic acid which plays a key role in bacterial sporulation process
33912
Escherichia coli
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.3.3.7
tetramer
4 * 32000, Lys161 is the active site, SDS-PAGE
Escherichia coli