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Literature summary for 4.3.3.7 extracted from

  • Laber, B.; Gomis-Rueth, F.X.; Romao, M.J.; Huber, R.
    Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization (1992), Biochem. J., 268, 691-695.
No PubMed abstract available
Search for more literature for 4.3.3.7

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
3-Bromopyruvate
-
 Escherichia coli
dipicolinic acid 1.2 mM, 50% inhibition Escherichia coli
L-lysine 1 mM, 50% inhibition Escherichia coli
S-(2-aminoethyl)-L-cysteine 4.6 mM, 50% inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.55
-
 DL-aspartate-4-semialdehyde
-
 Escherichia coli
0.57
-
 pyruvate
-
 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
 4 * 32000, Lys161 is the active site, SDS-PAGE Escherichia coli
112000
-
 gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate-4-semialdehyde + pyruvate Escherichia coli synthesis of the precursor of dipicolinic acid which plays a key role in bacterial sporulation process ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
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
a

Storage Stability

Storage Stability Organism
-20°C, addition of glycerol, several months, no loss of activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate-4-semialdehyde + pyruvate
-
 Escherichia coli dihydrodipicolinate + H2O
-
 ?
L-aspartate-4-semialdehyde + pyruvate synthesis of the precursor of dipicolinic acid which plays a key role in bacterial sporulation process Escherichia coli ?
-
 ?
pyruvate + DL-aspartate-4-semialdehyde
-
 Escherichia coli (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 32000, Lys161 is the active site, SDS-PAGE Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1
-
 L-lysine
-
 Escherichia coli
1.2
-
 dipicolinic acid
-
 Escherichia coli
4.6
-
 S-(2-aminoethyl)-L-cysteine
-
 Escherichia coli