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

BRENDA support

Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 2-oxobutyrate competitive inhibitor of DHDPS Escherichia coli
4.3.3.7 2-oxoglutarate competitive inhibitor of DHDPS Escherichia coli
4.3.3.7 3-Fluoropyruvate competitive inhibitor of DHDPS, and a competitive substrates Escherichia coli
4.3.3.7 3-hydroxypyruvate competitive inhibitor of DHDPS and a competitive substrate Escherichia coli
4.3.3.7 Bromopyruvate is an irreversible inhibitor of DHDPS Escherichia coli
4.3.3.7 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.1.8 additional information Escherichia coli DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate ?
-
 ?
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate Escherichia coli
-
 (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.8 Escherichia coli
-
-
-
4.3.3.7 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.8 additional information DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate Escherichia coli ?
-
 ?
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate
-
 Escherichia coli (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.17.1.8 More crystal structure modelling and analysis, PDB ID 1ARZ, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.17.1.8 DHDPR
-
 Escherichia coli
4.3.3.7 DHDPS
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.3.7 23
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.1.8 8
-
 dehydration assay at Escherichia coli
4.3.3.7 8
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
1.17.1.8 metabolism DHDPR is central to the diaminopimelate pathway for lysine biosynthesis Escherichia coli
1.17.1.8 additional information NMR studies uncover that dihydrodipicolinate reductase is also a dehydratase, overview Escherichia coli