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Literature summary extracted from

  • Sowole, M.A.; Simpson, S.; Skovpen, Y.V.; Palmer, D.R.; Konermann, L.
    Evidence of allosteric enzyme regulation via changes in conformational dynamics A hydrogen/deuterium exchange investigation of dihydrodipicolinate synthase (2016), Biochemistry, 55, 5413-5422 .
    View publication on PubMed

Application

EC Number Application Comment Organism
4.3.3.7 drug development the enzyme is a promising antibiotic target Campylobacter jejuni
4.3.3.7 pharmacology the enzyme is a promising antibiotic target Campylobacter jejuni

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 bis-lysine
-
 Campylobacter jejuni
4.3.3.7 L-lysine allosteric inhihitor. Allostery is mediated by changes in the extent of thermally activated conformational fluctuations Campylobacter jejuni

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Campylobacter jejuni
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.3.7 pyruvate + L-aspartate-4-semialdehyde
-
 Campylobacter jejuni (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.3.7 tetramer
-
 Campylobacter jejuni

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 CjDHDPS
-
 Campylobacter jejuni

General Information

EC Number General Information Comment Organism
4.3.3.7 metabolism the enzyme catalyzes a step of the diaminopimelate biosynthetic pathway of lysine Campylobacter jejuni