4.3.3.7: 4-hydroxy-tetrahydrodipicolinate synthase
This is an abbreviated version!
For detailed information about 4-hydroxy-tetrahydrodipicolinate synthase, go to the full flat file.
Word Map on EC 4.3.3.7
-
4.3.3.7
-
diaminopimelate
-
4.2.1.52
-
s-lysine
-
drug development
-
homoserine
-
meso-diaminopimelate
-
aspartokinase
-
l-threonine
-
s-aspartate
-
s-2-aminoethyl-l-cysteine
-
feedback-insensitive
-
lysine-insensitive
-
beta-semialdehyde
-
pharmacology
-
l-aspartate-beta-semialdehyde
-
2.7.2.4
-
aspartate-derived
-
medicine
-
synthesis
-
agriculture
-
biotechnology
-
industry
-
food industry
- 4.3.3.7
- diaminopimelate
-
4.2.1.52
-
s-lysine
- drug development
- homoserine
- meso-diaminopimelate
- aspartokinase
- l-threonine
-
s-aspartate
- s-2-aminoethyl-l-cysteine
-
feedback-insensitive
-
lysine-insensitive
- beta-semialdehyde
- pharmacology
-
l-aspartate-beta-semialdehyde
-
2.7.2.4
-
aspartate-derived
- medicine
- synthesis
- agriculture
- biotechnology
- industry
- food industry
Reaction
Synonyms
Aq_1143, AT2G45440, BA3935 gene product, cDHDPS, CjDHDPS, DapA, DapA2, DHDPA synthase, DHDPS, DHDPS2, dihydro-dipicolinic acid synthase, dihydrodipicolinate synthase, dihydrodipicolinic acid synthase, dihydrodipocolinate synthase, dihydropicolinate synthetase, EC 4.2.1.52, FaDHDPS, HTPA synthase, More, MosA, MosA protein, MRSA-DHDPS, PA1010, pyruvate-aspartic semialdehyde condensing enzyme, Rv2753c, synthase, dihydrodipicolinate, VEG81, Vegetative protein 81
ECTree
4.3.3.7 4-hydroxy-tetrahydrodipicolinate synthaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 4.3.3.7 - 4-hydroxy-tetrahydrodipicolinate synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(1SR,3R,5S)-1-hydroxy-3,5-bis(methoxycarbonyl)thiomorpholin-1-ium
-
30 mM, 18% inhibition
(1SS,3R,5S)-1-hydroxy-3,5-bis(methoxycarbonyl)thiomorpholin-1-ium
-
9 mM, 48% inhibition
(3R,5R)-thiomorpholine-3,5-dicarboxylic acid 1,1-dioxide
-
50 mM, 11% inhibition
(3R,5S)-thiomorpholine-3,5-dicarboxylic acid 1,1-dioxide
-
50 mM, 14% inhibition
(S)-aspartate-4-semialdehyde
substrate inhibition
(S)-Lys
partial mixed inhibition with respect to pyruvate and partial non-competitive inhibition with resoect to L-aspartate 4-semialdehyde
2-(4-carbamoylphenyl)-2-oxoacetic acid
maximal inhibition of 15% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
2-hydroxyheptanediamide
maximal inhibition of 21% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
2-hydroxyheptanedioic acid
maximal inhibition of 74% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
2-oxohexanedioic acid
maximal inhibition of 40% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
2-oxopentanedioic acid
maximal inhibition of 15% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
2-oxopimelate
maximal inhibition of 88% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase. This assay is able to measure DapA enzyme kinetics if the dihydrodipicolinate reductase DapB is present in excess, because under these conditions DapA becomes rate limiting
2-phenoxyacetic acid
maximal inhibition of 4% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
3-Fluoropyruvate
-
competitive inhibitor of DHDPS, and a competitive substrates
3-hydroxy-2-oxopropanoate
time-dependent inhibition, qualitatively followed by mass spectrometry, initial noncovalent adduct formation, followed by the slow formation of the covalent adduct
3-hydroxypyruvate
-
competitive inhibitor of DHDPS and a competitive substrate
4-((2-amino-2-oxoethyl)sulfonyl) butanoic acid
maximal inhibition of 29% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
4-((2-amino-2-oxoethyl)thio)butanoic acid
maximal inhibition of 15% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
4-(2,4,5-trioxoimidazolidin-1-yl)butanoic acid
maximal inhibition of 21% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
4-amino benzoic acid
maximal inhibition of 8% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
4-amino-2-hydroxybenzoic acid
maximal inhibition of 4% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
4-[amino(oxo)acetyl]benzoic acid
maximal inhibition of 34% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
4-[carboxy(hydroxy)methyl]benzoic acid
maximal inhibition of 35% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
4-[methyl(oxalo)amino]butanoic acid
maximal inhibition of 39% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
5-(carbamoylamino)-5-oxopentanoic acid
maximal inhibition of 40% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
5-(carbamoylthio)pentanoic acid
maximal inhibition of 65% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
5-butylpyridine-2-carboxylic acid
maximal inhibition of 5% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
7-ethoxy-6,7-dioxoheptanoic acid
maximal inhibition of 35% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
benzoic acid
maximal inhibition of 2% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
bislysine
-
bislysine is a mixed partial inhibitor with respect to the first substrate, pyruvate, and a noncompetitive partial inhibitor with respect to L-aspartate-4-semialdehyde
carboxycarbonyl-benzoic acid
maximal inhibition of 22% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
dimethyl (3R,5S)-thiomorpholine-3,5-dicarboxylate 1,1-dioxide
-
20 mM, 19% inhibition; 20 mM, 6% inhibition
dimethyl chelidamate
-
IC50: 14 mM. 99% inhibition at 50 mM, noncompetitive with respect to both substrates
dimethyl-(2E,2'E)-2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate]
-
slow inhibition
dimethyl-2,2'-(2-hydroxy-1,3-phenylene)bis(2-oxoacetate)
-
slow-tight inhibition
ethyl 4-((2-amino-2-oxoethyl)sulfinyl)butanoate
maximal inhibition of 31% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
ethyl 4-((2-amino-2-oxoethyl)sulfonyl)butanoate
maximal inhibition of 12% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
ethyl 4-((2-amino-2-oxoethyl)thio)butanoate
maximal inhibition of 21% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
ethyl 5-(carbamoylsulfanyl)pentanoate
maximal inhibition of 34% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
ethyl [(4-amino-4-oxobutyl)(methyl)amino](oxo)acetate
maximal inhibition of 35% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
heptanedioic acid
maximal inhibition of 10% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
hydroxy[4-(methoxycarbonyl)phenyl]acetic acid
maximal inhibition of 35% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
L-aspartate
competitive inhibition, L-aspartate 4-semialdehyde as varied substrate
lysine
inhibition of wild-type DHDPS by lysine with respect to pyruvate is partial and uncompetitive, and partial non-competitive with respect to L-aspartate 4-semialdehyde. Ethanolamine, n-butylamine, 1-amino-2-propanol, 3-amino-1-propanol, iso-butylamine and Tris-HCl cannot rescue activity
methoxycarbonyl-phenyloxoacetic acid
maximal inhibition of 29% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
methyl 3-oxohexanoate
maximal inhibition of 5% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
methyl 4-(2,4,5-trioxoimidazolidin-1-yl)butanoate
maximal inhibition of 38% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
methyl 4-[(2-ethoxy-2-oxoethyl)(methyl)amino]butanoate
maximal inhibition of 42% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
-
methyl 4-[amino(oxo)acetyl]benzoate
maximal inhibition of 35% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
methyl 5-(carbamoylamino)-5-oxopentanoate
maximal inhibition of 65% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
methyl 6-oxo-6-(2H-tetrazol-5-yl)hexanoate
maximal inhibition of 35% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
methyl 7-amino-6,7-dioxoheptanoate
maximal inhibition of 24% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
methyl 7-amino-6-hydroxy-7-oxoheptanoate
maximal inhibition of 28% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
N1-(4-amino-4-oxobutyl)-N1-methylethanediamide
maximal inhibition of 40% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
NaBH4
NaBH4 reduction of the pyruvyl-Schiff-base intermediate results in enzyme inactivation
oxaloacetate
non-competitive inhibition, pyruvate as varied substrate
pyruvate
substrate inhibition
Sodium borohydride
wild-type DHDPS is inactivated when incubated with pyruvate, whereas incubation with L-aspartate 4-semialdehyde has no effect
Succinate-semialdehyde
reversible inhibitor which is competitive with respect to L-aspartate-4-semialdehyde and uncompetitive with respect to pyruvate
[(4-amino-4-oxobutyl)(methyl)amino](oxo)acetic acid
maximal inhibition of 44% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase
(2R,6S)-piperidine-2,6-dicarboxylic acid
-
IC50: 20 mM, 83% inhibition at 50 mM
(2R,6S)-piperidine-2,6-dicarboxylic acid
-
20 mM, 43% inhibition; 20 mM, 77% inhibition
(S)-lysine
allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition; allosteric feedback inhibition, allosteric site modeling; allosteric feedback inhibition, allosteric site modeling; allosteric feedback inhibition, allosteric site modeling; allosteric feedback inhibition, allosteric site modeling
(S)-lysine
increasing amounts of (S)-lysine (0-200 mM) added, not inhibited under physiological conditions, binding site of the allosteric inhibitor lysine appears not to be conserved
(S)-lysine
-
feedback inhibition, the tetrameric enzyme has two allosteric sites, each of which binds two molecules of lysine. Lysine binds highly cooperatively, and primarily to the F form of the enzyme during the ping-pong mechanism. (S)-Lysine is an uncompetitive partial inhibitor with respect to its first substrate, pyruvate, and a mixed partial inhibitor with respect to its second substrate, (S)-aspartate-4-semialdehyde
(S)-lysine
mutant enzymes R138H and R138A show the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
(S)-lysine
-
partial mixed inhibition with respect to its first substrate, pyruvate
(S)-lysine
partial mixed inhibition with respect to (S)-aspartate 4-semialdehyde, partial non-ncompetitive inhibition with respect to pyruvate in wild-type and in Y107W mutant, Y107W mutant still retains over 25% of uninhibited activity, even at high inhibitor concentrations compared to the wild-type enzyme retaining less than 10% of normal activity
(S)-lysine
-
feedback inhibition, feedback inhibition of the Escherichia coli enzyme by lysine is successfully alleviated after substitution of the residues around the inhibitor's binding sites with those of the Corynabacterium glutamicum enzyme
(S)-lysine
no significant conformational change between the pyruvate-bound and (S)-lysine-bound enzyme, presence of substrate has substantial effect on the nature of enzyme-inhibitor association, solvent plays a key role in binding of inhibitor
2-oxobutyrate
forms a Schiff base with MosA protein, competitive inhibition
3-Bromopyruvate
competitive inhibition, pyruvate as varied substrate
4-oxo-1,4-dihydropyridine-2,6-dicarboxylic acid
-
i.e. chelidamic acid, IC50: 22 mM, 99% inhibition at 50 mM, uncompetitive inhibitor with respect to both substrates
4-oxo-1,4-dihydropyridine-2,6-dicarboxylic acid
-
20 mM, 73% inhibition
4-oxo-1,4-dihydropyridine-2,6-dicarboxylic acid
-
20 mM, 83% inhibition
cis-(1SS,3R5S)-3,5-thiomorpholinedicarboxylic acid, dimethyl ester, 1-oxide
-
20 mM, 8% inhibition
cis-(1SS,3R5S)-3,5-thiomorpholinedicarboxylic acid, dimethyl ester, 1-oxide
-
20 mM, 8% inhibition
cis-(1SS,3R5S)-3,5-thiomorpholinedicarboxylic acid, dimethyl ester, 1-oxide
-
20 mM, 10% inhibition
dimethyl (2R,6S)-piperidine-2,6-dicarboxylate
-
20 mM, 24% inhibition; 20 mM, 99% inhibitione
dimethyl (3R,5R)-thiomorpholine-3,5-dicarboxylate
-
20 mM, 19% inhibition
dimethyl (3R,5R)-thiomorpholine-3,5-dicarboxylate 1,1-dioxide
-
50 mM, 12% inhibition
dimethyl (3R,5R)-thiomorpholine-3,5-dicarboxylate 1,1-dioxide
-
20 mM, 14% inhibition
dimethyl (3R,5R)-thiomorpholine-3,5-dicarboxylate 1,1-dioxide
-
20 mM, 6% inhibition; 20 mM, 7% inhibition
dimethyl (3R,5R)-thiomorpholine-3,5-dicarboxylate 1-oxide
-
20 mM, 7% inhibition
dimethyl (3R,5R)-thiomorpholine-3,5-dicarboxylate 1-oxide
-
20 mM, 7% inhibition
dimethyl (3R,5S)-thiomorpholine-3,5-dicarboxylate
-
20 mM, 23% inhibition
dimethyl 4-oxo-1,4-dihydropyridine-2,6-dicarboxylate
-
20 mM, 84% inhibition
dimethyl 4-oxo-1,4-dihydropyridine-2,6-dicarboxylate
-
20 mM, 88% inhibition
L-aspartate 4-semialdehyde
Q81WN7
DHDPS is subject to substrate inhibition by L-aspartate 4-semialdehyde
L-aspartate 4-semialdehyde
uncompetitive inhibition by high concentrations of, no overcome by increasing pyruvate concentrations from 5 to 15 mM
L-aspartate 4-semialdehyde
competitive inhibition at high substrate concentrations
L-aspartate 4-semialdehyde
is subject to substrate inhibition by high concentrations
L-lysine
-
allosteric inhihitor. Allostery is mediated by changes in the extent of thermally activated conformational fluctuations
L-lysine
lack of feedback inhibition, not regulated under normal physiological conditions
L-lysine
no difference in its sensitivity or behaviour with respect to L-lysine when compared to the wild-type
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
L-lysine
-
inhibition of the tetrameric wild-type enzyme, but not of the disrupted minimeric mutant enzyme. Allosteric binding by two molecules of (S)-lysine at the DHDPS tight-dimer interface cleft has been observed to operate via a cooperative mechanism and to result in incomplete partial mixed inhibition, inhibition kinetics, overview
L-lysine
is significantly more sensitive to feedback inhibition than Escherichia coli DHDPS
L-lysine
binds at three sites to the enzyme, binding structure, overview
L-lysine
feedback inhibition, binding of lysine to the allosteric cleft of the enzyme, cooperative binding, structural mechanism for allosteric inhibition, overview. With respect to L-aspartate-4-semialdehyde, lysine is a noncompetitive inhibitor
L-threonine
-
at 100 mM 23% residual activity, at 100 mM 33% residual activity
pyridine-2,6-dicarboxylic acid
-
20 mM, 75% inhibition; 20 mM, 80% inhibition
Succinic semialdehyde
uncompetitive inhibition, L-aspartate 4-semialdehyde as varied substrate
trans-(1SS,3R5S)-3,5-thiomorpholinedicarboxylic acid, dimethyl ester, 1-oxide
-
20 mM, 20% inhibition
trans-(1SS,3R5S)-3,5-thiomorpholinedicarboxylic acid, dimethyl ester, 1-oxide
-
20 mM, 14% inhibition; 20 mM, 22% inhibition
trans-(1SS,3R5S)-3,5-thiomorpholinedicarboxylic acid, dimethyl ester, 1-oxide
-
20 mM, 12% inhibition
additional information
Q81WN7
is not inhibited by 1-100 mM L-lysine or L-isoleucine
-
additional information
-
is not inhibited by 1-100 mM L-lysine or L-isoleucine
-
additional information
-
not inhibitory: ATP, ADP, AMP, citric acid, L-malic acid, 2-oxoglutaric acid, fumaric acid, succinic acid, L-glutamic acid, L-threonine
-
additional information
-
no inhibition by (S)-aspartate 4-semialdehyde, but inhibition occurs by a derivative that is built of the compounbd in the enzyme preparation by ozonolysis
-
additional information
-
no inhibition by dipicolinic acid methyl ester, (3R,5S)-thiomorpholine-3,5-dicarboxylic acid compound 20b, (3R,5R)-thiomorpholine-3,5-dicarboxylic acid, compound 23, compound 24b, dimethyl (3R,5S)thiomorpholine-3,5-dicarboxylate 1,1-dioxide
-
additional information
inhibition studies by using 4-oxo-heptenedioic acid analogues, determination of second-order rate constants of inactivation, substrate co-incubation studies show that the inhibitors act at the active-site, interaction analyzed by mass spectrometry, sites of enzyme alkylation determined
-
additional information
new constrained inhibitors of DHDPS identified and tested, time-dependent inhibition and substrate protection, dimethyl 2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate] discovered as a relatively potent inhibitor of DHDPS enzyme, validates constrained acyclic-intermediate model as a potential inhibitor lead, modifications of the aromatic ring are possible and may result in improvements in activity
-
additional information
-
no substrate inhibition by (S)-aspartate 4-semialdehyde
-
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
-
additional information
-
1,3-phenylene bis(ketoacid) derivatives as enzyme inhibitors, overview. Ketoacid derivatives act as slow and slow-tight binding inhibitors with either an encounter complex or a condensation product for the slow and slow-tight binding inhibitors, respectively, modeling, overview. No or poor inhibition by dimethyl 2,2'-benzene-1,3-diylbis(oxoacetate), (2E,2'E)-2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoic acid], and dimethyl-2,2'-(2-methoxy-1,3-phenylene)bis(2-oxoacetate)
-
additional information
molecular descriptors analysis shows that ligands with polar surface area of 91.7 A are likely inhibitors
-
additional information
-
molecular descriptors analysis shows that ligands with polar surface area of 91.7 A are likely inhibitors
-
additional information
-
not inhibitory: iodoacetate, iodoacetamide, p-chloromercuribenzoate
-
additional information
not inhibited by (S)-lysine, suggesting that feedback control of the lysine biosynthetic pathway evolves later in the bacterial lineage
-
additional information
-
not inhibited by (S)-lysine, suggesting that feedback control of the lysine biosynthetic pathway evolves later in the bacterial lineage
-
additional information
-
is insensitive to L-lysine inhibition, produces no binding isotherm upon L-lysine addition in either the absence or presence of pyruvate
-
