Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.3.3.7 extracted from

  • Atkinson, S.C.; Dogovski, C.; Downton, M.T.; Czabotar, P.E.; Dobson, R.C.; Gerrard, J.A.; Wagner, J.; Perugini, M.A.
    Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition (2013), Plant Mol. Biol., 81, 431-446.
    View publication on PubMed
Search for more literature for 4.3.3.7

Cloned(Commentary)

Cloned (Comment) Organism
gene dapA, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Vitis vinifera

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of protein in 20 mM pyruvate and 20 mM lysine, with 0.002 ml of reservoir solution containing 0.1 M MES, pH 6.5, 6% v/v PEG 20000, X-ray diffraction structure determination and analysis at 2.40 A resolution Vitis vinifera

Inhibitors

Inhibitors Comment Organism Structure
L-lysine feedback inhibition, binding of lysine to the allosteric cleft of the enzyme, cooperative binding, structural mechanism for allosteric inhibition, overview. With respect to L-aspartate-4-semialdehyde, lysine is a noncompetitive inhibitor Vitis vinifera

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Vitis vinifera

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate + L-aspartate-4-semialdehyde Vitis vinifera
-
 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Vitis vinifera D7U7T8 gene dapA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography Vitis vinifera

Reaction

Reaction Comment Organism Reaction ID
pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O the reaction proceeds via a ping-pong kinetic mechanism in which pyruvate binds and forms a Schiff base to an active-site lysine residue (Lys184 in Vitis vinifera enzyme). L-aspartate-4-semialdehyde then reacts with the resultant enamine and following cyclization forms the product (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate Vitis vinifera
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information coupled assay with dihydrodipicolinate reductase Vitis vinifera ?
-
 ?
pyruvate + L-aspartate-4-semialdehyde
-
 Vitis vinifera (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
 ?

Subunits

Subunits Comment Organism
homotetramer homotetramer of four identical (beta/alpha)8-barrel monomers, a dimer of tight dimers, with two tight-dimers binding in a head-to-head manner, with the active site situated near the center of the barrel, molecular dynamics simulations Vitis vinifera

Synonyms

Synonyms Comment Organism
DHDPS
-
 Vitis vinifera
dihydrodipicolinate synthase
-
 Vitis vinifera

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Vitis vinifera

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Vitis vinifera

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information kinetic and thermodynamics of allosteric inhibitin by lysine, overview Vitis vinifera
0.049
-
 L-lysine versus L-aspartate-4-semialdehyde, pH 8.0, 30°C, recombinant enzyme Vitis vinifera

General Information

General Information Comment Organism
metabolism lysine biosynthesis in plants is tightly regulated by feedback inhibition of the end product on dihydrodipicolinate synthase, the first enzyme of the lysine-specific branch Vitis vinifera