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Literature summary for 4.3.3.7 extracted from

  • Devenish, S.R.; Blunt, J.W.; Gerrard, J.A.
    NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase (2010), J. Med. Chem., 53, 4808-4812.
    View publication on PubMed
Search for more literature for 4.3.3.7

Inhibitors

Inhibitors Comment Organism Structure
2-oxobutyrate competitive inhibitor of DHDPS Escherichia coli
2-oxoglutarate competitive inhibitor of DHDPS Escherichia coli
3-Fluoropyruvate competitive inhibitor of DHDPS, and a competitive substrates Escherichia coli
3-hydroxypyruvate competitive inhibitor of DHDPS and a competitive substrate Escherichia coli
Bromopyruvate is an irreversible inhibitor of DHDPS Escherichia coli
additional information the substrate specificity of the enzyme, two pyruvate analogues, previously classified as weak competitive inhibitors, are turned over productively by DHDPS, NMR spectroscopy, overview 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
-
 (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate 4-semialdehyde + pyruvate
-
 Escherichia coli (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
 ?

Synonyms

Synonyms Comment Organism
DHDPS
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli