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Literature summary for 4.3.3.7 extracted from

  • Muscroft-Taylor, A.C.; Soares da Costa, T.P.; Gerrard, J.A.
    New insights into the mechanism of dihydrodipicolinate synthase using isothermal titration calorimetry (2010), Biochimie, 92, 254-262.
    View publication on PubMed
Search for more literature for 4.3.3.7

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant cloned into plasmid pET-151/D-TOPO and expressed in Escherichia coli BL21 Star (DE3) competent cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
K161A substantially diminished binding affinity of pyruvate, the surrounding active site scaffold is unable to compensate the entropic penalty associated with ligand localisation in the absence of Schiff-base formation Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-aspartate 4-semialdehyde competitive inhibition at high substrate concentrations Escherichia coli
L-lysine binding interaction of L-lysine is characterised as a cooperative event in which an entropic pre-organisation step precedes a secondary enthalpic association. This allosteric association is of a mixed competitive nature in which heterotropic ligand cooperativity is observed to subtly influence the binding events Escherichia coli
additional information is insensitive to L-lysine inhibition, produces no binding isotherm upon L-lysine addition in either the absence or presence of pyruvate Thermotoga maritima
NaBH4 NaBH4 reduction of the pyruvyl-Schiff-base intermediate results in enzyme inactivation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6L2
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Thermotoga maritima
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Purification (Commentary)

Purification (Comment) Organism
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 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate 4-semialdehyde + pyruvate pyruvate is a weak binder (0.023 mM) and L-aspartate 4-semialdehyde does not interact with the enzyme in the absence of a Schiff-base with pyruvate. Lys161 plays a crucial role in providing the thermodynamic force for the association of pyruvate with the DHDPS active site Escherichia coli dihydrodipicolinate + 2 H2O
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 ?

Synonyms

Synonyms Comment Organism
DHDPS
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 Thermotoga maritima
DHDPS
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 Escherichia coli
dihydrodipicolinate synthase
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 Thermotoga maritima
dihydrodipicolinate synthase
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 Escherichia coli