1.17.1.8: 4-hydroxy-tetrahydrodipicolinate reductase
This is an abbreviated version!
For detailed information about 4-hydroxy-tetrahydrodipicolinate reductase, go to the full flat file.
Word Map on EC 1.17.1.8
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1.17.1.8
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diaminopimelate
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glutamicum
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meso-diaminopimelate
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aspartokinase
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imine
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dhdps
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2,6-pyridinedicarboxylate
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medicine
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alpha,beta-unsaturated
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2'-phosphate
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s-2-aminoethyl-l-cysteine
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aspartate-semialdehyde
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drug development
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agriculture
- 1.17.1.8
- diaminopimelate
- glutamicum
- meso-diaminopimelate
- aspartokinase
- imine
- dhdps
- 2,6-pyridinedicarboxylate
- medicine
-
alpha,beta-unsaturated
-
2'-phosphate
- s-2-aminoethyl-l-cysteine
-
aspartate-semialdehyde
- drug development
- agriculture
Reaction
Synonyms
AbDHDPR, CRR1, DapB, DHDP reductase, DHDPR, DHPR, dihydrodipicolinate reductase, dihydrodipicolinate reductase-like protein, dihydrodipicolinic acid reductase, EC 1.3.1.26, MRSA-DHDPR, reductase, dihydrodipicolinate
ECTree
1.17.1.8 4-hydroxy-tetrahydrodipicolinate reductaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 1.17.1.8 - 4-hydroxy-tetrahydrodipicolinate reductase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2,3-dihydrodipicolinate
the enzyme is inhibited by high concentrations of 2,3-dihydrodipicolinate
2,6-pyridine dicarboxylate
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stable analog of the dihydrodipicolinate substrate, the binding affinity is not affected by the presence of NADH or NAD+
2,6-pyridinedicarboxylate
competitive, binding site structure
dihydrodipicolinate
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the enzyme is inhibited by high concentrations of dihydrodipicolinate when using NADPH as a cofactor, but not with NADH
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate
dihydrodipicolinate reductase enzymes from plants are much more prone to substrate inhibition than the bacterial enzymes, which appears to be a consequence of increased flexibility of the substrate-binding loop and higher affinity for the nucleotide substrate
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate
dihydrodipicolinate reductase enzymes from plants are much more prone to substrate inhibition than the bacterial enzymes, which appears to be a consequence of increased flexibility of the substrate-binding loop and higher affinity for the nucleotide substrate
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate
dihydrodipicolinate reductase enzymes from plants are much more prone to substrate inhibition than the bacterial enzymes, which appears to be a consequence of increased flexibility of the substrate-binding loop and higher affinity for the nucleotide substrate
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate
when NADPH is employed as the cofactor
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate
dihydrodipicolinate reductase enzymes from plants are much more prone to substrate inhibition than the bacterial enzymes, which appears to be a consequence of increased flexibility of the substrate-binding loop and higher affinity for the nucleotide substrate
dipicolinate
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non-competitively versus dihydrodipicolinate, competitive versus NADPH
dipicolinate
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non-competitively versus dihydrodipicolinate, competitive versus NADPH; positive cooperativity
dipicolinate
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reversible, competitive versus substrate (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate
dipicolinate
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non-competitively versus dihydrodipicolinate, competitive versus NADPH
isophthalic acid
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reversible, competitive versus substrate 2,3-dihydrodipicolinate
additional information
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no regulation of enzyme by amino acids from the aspartate family
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additional information
neither repression nor inhibition by the end products of lysine biosynthetic pathway
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additional information
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not inhibited by lysine, methionine and threonine
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additional information
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investigation of inhibitory potential of diverse heterocyclic and aromatic compounds, overview
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