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Literature summary for 4.3.3.7 extracted from

  • Atkinson, S.C.; Dogovski, C.; Dobson, R.C.; Perugini, M.A.
    Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from Agrobacterium tumefaciens (2012), Acta Crystallogr. Sect. F, 68, 1040-1047.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene dapA, sequence comparison with Escherichia coli enzyme, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) Agrobacterium tumefaciens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged enzyme in the unliganded form and in forms with bound substrate and with bound substrate plus allosteric inhibitor lysine, hanging drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 20 mM Tris, pH 8.0, with 0.002 ml of reservoir solution containing 0.1 M Tris, pH 8.5, and 2 M ammonium sulfate, for ligand-bound enzyme from 0.17 M lithium sulfate monohydrate, 0.085 M Tris pH 8.5, 25.5%(w/v) PEG 4000, 15%(v/v) glycerol with addition of 20 mM pyruvate or 20 mM pyruvate and 20 mM lysine, equilibration against 1 ml reservoir solution, 20°C, overnight, X-ray diffraction structure determination and analysis at 1.40-1.55 A resolution Agrobacterium tumefaciens

Inhibitors

Inhibitors Comment Organism Structure
D-Lysine allosteric inhibitor Agrobacterium tumefaciens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-aspartate-4-semialdehyde + pyruvate Agrobacterium tumefaciens
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
?
(S)-aspartate-4-semialdehyde + pyruvate Agrobacterium tumefaciens C58 / ATCC 33970
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
?

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens Q8UGL3 gene dapA
-
Agrobacterium tumefaciens C58 / ATCC 33970 Q8UGL3 gene dapA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme 8fold from Escherichia coli strain BL21 (DE3) by immobilized metal affinity chromatography and gel filtration Agrobacterium tumefaciens

Reaction

Reaction Comment Organism Reaction ID
pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O ping-pong mechanism, in which pyruvate binds as a Schiff base to an active-site lysine residue (Lys162 in Agrobacterium tumefaciens) Agrobacterium tumefaciens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
174
-
purified recombinant His-tagged enzyme, coupled assay, pH and temperature not specified in the publication Agrobacterium tumefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-aspartate-4-semialdehyde + pyruvate
-
Agrobacterium tumefaciens (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
?
(S)-aspartate-4-semialdehyde + pyruvate
-
Agrobacterium tumefaciens C58 / ATCC 33970 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
?

Synonyms

Synonyms Comment Organism
DHDPS
-
Agrobacterium tumefaciens
dihydrodipicolinate synthase
-
Agrobacterium tumefaciens

General Information

General Information Comment Organism
metabolism the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid Agrobacterium tumefaciens