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(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
(S)-aspartate-4-semialdehyde + pyruvate
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + 2 H2O
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
pyruvate + L-aspartate-4-semialdehyde
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
(S)-aspartate-4-semialdehyde + pyruvate
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
L-aspartate 4-semialdehyde + pyruvate
(S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
-
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + 2 H2O
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
-
?
L-aspartate-4-semialdehyde + pyruvate
?
-
synthesis of the precursor of dipicolinic acid which plays a key role in bacterial sporulation process
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
pyruvate + (R,S)-aspartate-4-semialdehyde
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
-
?
pyruvate + DL-aspartate-4-semialdehyde
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
-
?
pyruvate + L-aspartate-4-semialdehyde
2,3-dihydrodipicolinate + ?
-
2,3-dihydrodipicolinate is the product of the synthase reaction. One or more of the NMR peaks previously assigned to the product of the dihydrodipicolinate synthase reaction, presumed to be (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate, actually arises from a non-enzymatic reaction
-
-
?
additional information
?
-
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
branch point reaction in the biosynthesis of lysine
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
biosynthesis of (S)-lysine and meso-diaminopimelate
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
diketopimelic acid derivatives designed as mimics of the acyclic enzyme-bound condensation product of (S)-aspartate 4-semialdehyde and pyruvate, inhibition analysis
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
reaction mechanism and active site analyzed, inhibition by the substrate analog beta-hydroxypyruvate
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
role of Tyr107 residue, located at the tight-dimer interface between two monomers, participates in a catalytic triad of residues during catalysis
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + 2 H2O
-
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + 2 H2O
-
-
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + 2 H2O
-
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + 2 H2O
condensation reaction between both substrates via the formation of a Schiff base intermediate between pyruvate and the absolutely conserved active-site lysine. Although lysine 161 is important in the wild-type DHDPS-catalysed reaction, it is not absolutely essential for catalysis
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + 2 H2O
pyruvate is a weak binder (0.023 mM) and L-aspartate 4-semialdehyde does not interact with the enzyme in the absence of a Schiff-base with pyruvate. Lys161 plays a crucial role in providing the thermodynamic force for the association of pyruvate with the DHDPS active site
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
branch poit of (S)-lysine biosynthesis
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
substrate protection and inhibition experiments
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
-
?
(S)-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
first step in the biosynthesis of lysine, overview
-
?
(S)-aspartate-4-semialdehyde + pyruvate
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
-
-
-
?
(S)-aspartate-4-semialdehyde + pyruvate
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O
-
the enzyme-catalyzed reaction is initiated by condensation of pyruvate with an active site Lys161 forming a Schiff base. Subsequent tautomerization to the enamine and aldol-type reaction with (S)-aspartate-4-semialdehyde then generates an acyclic enzyme-bound intermediate. Transimination of the acyclic intermediate yields the cyclic alcohol (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid, with simultaneous release of the active site lysine residue
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + 2 H2O
-
-
-
-
?
L-aspartate 4-semialdehyde + pyruvate
dihydrodipicolinate + 2 H2O
-
active sites are similiar to Bacillus anthracis DHDPS
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
L-aspartate-4-semialdehyde + pyruvate
dihydrodipicolinate + H2O
-
-
-
?
additional information
?
-
-
no reaction with oxaloacetic acid, phosphoenolpyruvate, glutamic semialdehyde, N-acetylaspartic semialdehyde, succinic semialdehyde
-
-
?
additional information
?
-
-
no activity with (R)-aspartate 4-semialdehyde
-
?
additional information
?
-
-
the quaternary structure plays a significant role in substrate specificity, overview
-
-
?
additional information
?
-
-
coupled assay with dihydrodipicolinate reductase
-
-
?
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(2E)-4-oxohept-2-enedioic acid
-
(2E,5E)-4-oxohepta-2,5-dienedioic acid
-
(S)-Lys
partial mixed inhibition with respect to pyruvate and partial non-competitive inhibition with resoect to L-aspartate 4-semialdehyde
2,2'-benzene-1,3-diylbis(oxoacetic acid)
-
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
diethyl (2E)-4-oxohept-2-enedioate
-
diethyl (2E,5E)-4-oxohepta-2,5-dienedioate
-
dimethyl 2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate]
-
L-aspartate 4-semialdehyde
competitive inhibition at high substrate concentrations
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
NaBH4
NaBH4 reduction of the pyruvyl-Schiff-base intermediate results in enzyme inactivation
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
(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
(2R,6S)-piperidine-2,6-dicarboxylic acid
(3R,5R)-thiomorpholine-3,5-dicarboxylic acid
-
50 mM, 32% 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
2,2'-(2-hydroxy-1,3-phenylene)bis(2-oxoacetic acid)
-
slow-tight inhibition
2,2'-benzene-1,3-diylbis(oxoacetic acid)
-
slow inhibition
2-oxobutyrate
-
competitive inhibitor of DHDPS
2-oxoglutarate
-
competitive inhibitor of DHDPS
3-fluoro-2-oxopropanoate
-
-
3-Fluoropyruvate
-
competitive inhibitor of DHDPS, and a competitive substrates
3-hydroxypyruvate
-
competitive inhibitor of DHDPS and a competitive substrate
4-oxo-1,4-dihydropyridine-2,6-dicarboxylic acid
Bromopyruvate
-
is an irreversible inhibitor of DHDPS
cis-(1SS,3R5S)-3,5-thiomorpholinedicarboxylic acid, dimethyl ester, 1-oxide
-
20 mM, 8% inhibition
cis-piperidine-2,6-dicarboxylic acid
-
and derivatives
dimethyl (2R,6S)-piperidine-2,6-dicarboxylate
-
20 mM, 92% inhibition
dimethyl (3R,5R)-thiomorpholine-3,5-dicarboxylate
-
20 mM, 12% inhibition
dimethyl (3R,5R)-thiomorpholine-3,5-dicarboxylate 1,1-dioxide
dimethyl (3R,5S)-thiomorpholine-3,5-dicarboxylate
dimethyl 4-oxo-1,4-dihydropyridine-2,6-dicarboxylate
-
-
dimethyl chelidamate
-
IC50: 14 mM. 99% inhibition at 50 mM, noncompetitive with respect to both substrates
dimethyl piperidine-2,6-dicarboxylate
-
-
dimethyl pyridine-2,6-dicarboxylate
-
20 mM, 5% inhibition
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
dipicolinic acid di-imidate
-
-
dipicolinic acid N-oxide
-
0.8 mM 50% inhibition
L-threonine
-
at 100 mM 23% residual activity, at 100 mM 33% residual activity
pyridine-2,6-dicarboxylic acid
-
-
S-(2-aminoethyl)-L-cysteine
-
4.6 mM, 50% inhibition
Succinic semialdehyde
-
-
trans-(1SS,3R5S)-3,5-thiomorpholinedicarboxylic acid, dimethyl ester, 1-oxide
-
20 mM, 20% inhibition
(S)-lysine
allosteric inhibitor
(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 (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
L-lysine
-
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
no difference in its sensitivity or behaviour with respect to L-lysine when compared to the wild-type
L-lysine
natural feedback inhibitor
(2R,6S)-piperidine-2,6-dicarboxylic acid
-
20 mM, 49% inhibition
(2R,6S)-piperidine-2,6-dicarboxylic acid
-
IC50: 20 mM, 83% inhibition at 50 mM
(S)-lysine
-
partial mixed inhibition with respect to its first substrate, pyruvate
(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
4-oxo-1,4-dihydropyridine-2,6-dicarboxylic acid
-
-
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
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,5S)-thiomorpholine-3,5-dicarboxylate
-
20 mM, 35% inhibition
dimethyl (3R,5S)-thiomorpholine-3,5-dicarboxylate
-
50 mM, 36% inhibition
dipicolinic acid
-
-
dipicolinic acid
-
1 mM, 50% inhibition
dipicolinic acid
-
1.2 mM, 50% inhibition
dipicolinic acid
-
IC50: 20 mM, competitive inhibitor
L-lysine
-
-
L-lysine
-
1 mM, 50% inhibition
L-lysine
-
at 1 mM 23% residual activity, at 100 mM 13% residual activity
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
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 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
-
1-100 mM L-isoleucine has no effect
-
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)
-
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0.09 - 2.7
(S)-aspartate 4-semialdehyde
0.12 - 37
L-aspartate 4-semialdehyde
0.21
(R,S)-aspartate-4-semialdehyde
-
pH 8.0, 30°C, with pyruvate
0.11
(S)-aspartate 4-semialdehyde
0.137 - 0.3
(S)-aspartate-4-semialdehyde
0.55
DL-aspartate-4-semialdehyde
-
-
0.11 - 0.14
L-aspartate 4-semialdehyde
0.25
L-aspartate-4-semialdehyde
-
-
additional information
additional information
-
0.09
(S)-aspartate 4-semialdehyde
mutant T44V, pH 8.0, 30°C
0.11
(S)-aspartate 4-semialdehyde
wild-type
0.11
(S)-aspartate 4-semialdehyde
wild-type enzyme, pH 8.0, 30°C
0.39
(S)-aspartate 4-semialdehyde
Y107W mutant
0.58
(S)-aspartate 4-semialdehyde
mutant Y107F, pH 8.0, 30°C
0.58
(S)-aspartate 4-semialdehyde
Y107F mutant
2.7
(S)-aspartate 4-semialdehyde
mutant Y133F, pH 8.0, 30°C
0.12
L-aspartate 4-semialdehyde
mutant K161R, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR
0.12
L-aspartate 4-semialdehyde
wild-type, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR
0.13
L-aspartate 4-semialdehyde
mutant T44S
0.13
L-aspartate 4-semialdehyde
wild-type, at 30°C
0.15
L-aspartate 4-semialdehyde
mutants Q196D, D193A and D193Y, at 30°C
0.17
L-aspartate 4-semialdehyde
mutant D193A, at 30°C
0.23
L-aspartate 4-semialdehyde
C-terminal truncated DHDPS (H225*), at 30°C, in 150 mM HEPES, pH 8.0, 0.16 mM NADPH, 50 microg/ml DHDPR
0.23
L-aspartate 4-semialdehyde
mutant K161A, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR
0.29
L-aspartate 4-semialdehyde
polyhistidine-tagged wild-type DHDPSR
5.1
L-aspartate 4-semialdehyde
mutant enzyme R138A
37
L-aspartate 4-semialdehyde
mutant enzyme R138H
0.08
pyruvate
mutant T44V, pH 8.0, 30°C
0.15
pyruvate
wild-type, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR
0.16
pyruvate
mutant Y107F, pH 8.0, 30°C
0.16
pyruvate
Y107F mutant
0.16
pyruvate
wild-type, at 30°C
0.26
pyruvate
wild-type enzyme, pH 8.0, 30°C
0.28
pyruvate
mutant enzyme R138H
0.32
pyruvate
mutant Q196D, at 30°C
0.36
pyruvate
polyhistidine-tagged wild-type DHDPS
0.37
pyruvate
C-terminal truncated DHDPS (H225*), at 30°C, in 150 mM HEPES, pH 8.0, 0.16 mM NADPH, 50 microg/ml DHDPR
0.44
pyruvate
mutant D193A, at 30°C
0.45
pyruvate
mutant enzyme R138A
0.45
pyruvate
mutant K161A, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR
0.46
pyruvate
mutant Q234D, at 30°C
0.57
pyruvate
mutant D193Y, at 30°C
0.57
pyruvate
mutant K161R, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR
0.92
pyruvate
mutant T44S
1.5
pyruvate
Y107W mutant
35
pyruvate
mutant Y133F, pH 8.0, 30°C
0.11
(S)-aspartate 4-semialdehyde
-
30°C
0.11
(S)-aspartate 4-semialdehyde
-
pH 8.0, 30°C, with pyruvate
0.137
(S)-aspartate-4-semialdehyde
-
recombinant mutant H56K, pH 8.0, temperature not specified in the publication
0.248
(S)-aspartate-4-semialdehyde
-
recombinant mutant E84T, pH 8.0, temperature not specified in the publication
0.3
(S)-aspartate-4-semialdehyde
-
recombinant wild-type enzyme, pH 8.0, temperature not specified in the publication
0.11
L-aspartate 4-semialdehyde
-
at 30°C, in 100 mM HEPES buffer, pH 8.0
0.14
L-aspartate 4-semialdehyde
-
pH 8.0
0.13
pyruvate
-
-
0.25
pyruvate
-
pH 8.0, 30°C, with (S)-aspartate 4-semialdehyde
0.26
pyruvate
-
at 30°C, in 100 mM HEPES buffer, pH 8.0
0.3
pyruvate
-
pH 8.0, 30°C, with (R,S)-aspartate 4-semialdehyde
0.556
pyruvate
-
recombinant mutant E84T, pH 8.0, temperature not specified in the publication
0.64
pyruvate
-
recombinant mutant H56K, pH 8.0, temperature not specified in the publication
0.827
pyruvate
-
recombinant wild-type enzyme, pH 8.0, temperature not specified in the publication
additional information
additional information
-
kinetic mechanism
-
additional information
additional information
-
kinetic study: the wild-type enzyme shows a ping pong mechanism, while the monomeric mutant L197D/Y107W shows ternary-complex mechanism
-
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32.4
(2E)-4-oxohept-2-enedioic acid
mono-ene inhibitor
1.63
(2E,5E)-4-oxohepta-2,5-dienedioic acid
more potent than the corresponding mono-ene inhibitors
2.96
2,2'-benzene-1,3-diylbis(oxoacetic acid)
49% inhibition at 5 mM, mimics the substrate pyruvate, binding with the active site lysine residue, slow inhibition
0.17
2-oxopimelic acid
in 50 mM Tris-HCl (pH 8.2), at 22°C
0.21
3-hydroxy-2-oxopropanoate
time-dependent inhibition, value similar to that of (S)-lysine
10.9
diethyl (2E)-4-oxohept-2-enedioate
mono-ene inhibitor
4.95
diethyl (2E,5E)-4-oxohepta-2,5-dienedioate
best inhibitor
0.33
dimethyl 2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate]
15% inhibition at 1 mM, binding with the active site lysine residue, kinetic analysis corresponds to slow-binding model of inhibition
0.3
Succinate-semialdehyde
in 50 mM Tris-HCl (pH 8.2), at 22°C
0.29
2,2'-(2-hydroxy-1,3-phenylene)bis(2-oxoacetic acid)
-
pH 8.0, 30°C
2.96
2,2'-benzene-1,3-diylbis(oxoacetic acid)
-
pH 8.0, 30°C
22 - 24.8
4-oxo-1,4-dihydropyridine-2,6-dicarboxylic acid
6.9 - 14
dimethyl chelidamate
0.33
dimethyl-(2E,2'E)-2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate]
-
pH 8.0, 30°C
0.04
dimethyl-2,2'-(2-hydroxy-1,3-phenylene)bis(2-oxoacetate)
-
pH 8.0, 30°C
0.8
dipicolinic acid N-oxide
-
-
4.6
S-(2-aminoethyl)-L-cysteine
-
-
0.32
(S)-Lys
with respect to L-aspartate 4-semialdehyde
3.9
(S)-Lys
with respect to pyruvate
0.18
L-lysine
mutant D193A, with respect to (S)-aspartate 4-semialdehyde
0.19
L-lysine
mutant Q196D, with respect to (S)-aspartate 4-semialdehyde
0.4
L-lysine
wild-type, with respect to (S)-aspartate 4-semialdehyde
2.2
L-lysine
mutant D193A, with respect to pyruvate
3.6
L-lysine
wild-type, with respect to pyruvate
4.1
L-lysine
mutant Q196D, with respect to pyruvate
0.12
lysine
wild-type, with pyruvate as substrate
0.14
lysine
mutant K161A, with pyruvate as substrate
0.14
lysine
mutant K161R, with L-aspartate 4-semialdehyde as substrate
0.14
lysine
mutant K161R, with pyruvate as substrate
0.18
lysine
wild-type, with L-aspartate 4-semialdehyde as substrate
0.23
lysine
mutant K161A, with L-aspartate 4-semialdehyde as substrate
0.32
(S)-lysine
-
versus (S)-aspartate 4-semialdehyde
3.9
(S)-lysine
-
versus pyruvate
22
4-oxo-1,4-dihydropyridine-2,6-dicarboxylic acid
-
with respect to pyruvate
24.8
4-oxo-1,4-dihydropyridine-2,6-dicarboxylic acid
-
with respect to L-aspartate 4-semialdehyde
6.9
dimethyl chelidamate
-
with respect to pyruvate
14
dimethyl chelidamate
-
with respect to L-aspartate 4-semialdehyde
1
dipicolinic acid
-
-
0.21
L-lysine
-
-
0.32
L-lysine
-
with (S)-aspartate 4-semialdehyde as substrate
3.9
L-lysine
-
with pyruvate as substrate
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0.0034
purified mutant T44V
0.008
purified mutant Y133F
0.27
purified mutant Y107F
0.72
crude extract of mutant T44S
1.81
purified wild-type enzyme
14.52
20.7fold purified mutant T44S
14.5
-
purified recombinant mutant L51K, pH 8.0, temperature not specified in the publication
19.2
-
purified recombinant mutant A49K, pH 8.0, temperature not specified in the publication
454.2
-
purified recombinant mutant H56K, pH 8.0, temperature not specified in the publication
478.1
-
purified recombinant mutant E84T, pH 8.0, temperature not specified in the publication
500.8
-
purified recombinant wild-type enzyme, pH 8.0, temperature not specified in the publication
559.4
-
purified recombinant mutant A49P, pH 8.0, temperature not specified in the publication
60.5
-
purified recombinant mutant L51T, pH 8.0, temperature not specified in the publication
81.6
-
purified recombinant mutant A49W, pH 8.0, temperature not specified in the publication
additional information
attempt to examine the specificity of the active site of DHDPS, co-crystallization with the substrate analogue oxaloacetate, solution of the protein structure indicates that pyruvate rather than oxaloacetic acid bounds in the active site, decarboxylation of oxaloacetate not catalysed by DHDPS, rate of pyruvate production independent of DHDPS concentration, indicating that the decarboxylation of oxaloacetate is occurring by a spontaneous and enzyme-independent mechanism, confirmed by kinetic analysis
additional information
-
attempt to examine the specificity of the active site of DHDPS, co-crystallization with the substrate analogue oxaloacetate, solution of the protein structure indicates that pyruvate rather than oxaloacetic acid bounds in the active site, decarboxylation of oxaloacetate not catalysed by DHDPS, rate of pyruvate production independent of DHDPS concentration, indicating that the decarboxylation of oxaloacetate is occurring by a spontaneous and enzyme-independent mechanism, confirmed by kinetic analysis
additional information
role of beta-hydroxypruvate in regulating biosynthesis of dihydrodipicolinate unknown, crystal structure of DHDPS enzyme complexed with beta-hydroxypyruvate solved, active site shows the presence of the inhibitor covalently bound to Lys161, hydroxyl group of inhibitor is hydrogen-bonded to main-chain carbonyl of Ile203, evidence for a catalytic function played by this peptide unit, highly strained torsion angle conserved in active site of other homologous enzyme, points to critical role in catalysis
additional information
-
role of beta-hydroxypruvate in regulating biosynthesis of dihydrodipicolinate unknown, crystal structure of DHDPS enzyme complexed with beta-hydroxypyruvate solved, active site shows the presence of the inhibitor covalently bound to Lys161, hydroxyl group of inhibitor is hydrogen-bonded to main-chain carbonyl of Ile203, evidence for a catalytic function played by this peptide unit, highly strained torsion angle conserved in active site of other homologous enzyme, points to critical role in catalysis
additional information
role of Tyr107 residue in determining the quaternary structure, structural, biophysical, and kinetic studies of the Y107W mutant, catalytic ability and apparent melting temperature reduced by the mutation, tetrameric quaternary structure critical to control specificity, heat stability, and intrinsic activity
additional information
substrate protection experiments, inhibition by alkylation the active-site lysine residue (Lys161) and a surface cysteine residue, slower alkylation of other cysteine residues with lower surface accessibility, co-incubation of the enzyme with the inhibitors in the presence of pyruvate protect against active-site alkylation and cysteine residues
additional information
-
-
additional information
-
-
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D193A
removal of water mediated hydrogen-bond network
D193Y
removal of water mediated hydrogen-bond network and introduction of steric bulk to alter surface topology
H118Y
mutant enzyme H56K is more conducive to L-lysine production than mutant H118Y
H56K
mutant enzyme H56K is more conducive to L-lysine production than mutant H118Y
K161R
catalytically active, significant decrease in activity. Is not inactivated when incubated with pyruvate and the reducing agent sodium borohydride. Negligible heat production associated with pyruvate binding to the mutant enzyme, consistent with the lack of Schiff base formation
Q196D
removal of hydrogen bonds and charge-charge repulsion, shortened side chain places charged carboxyl groups proximal at interface
Q234D
removal of hydrogen bond and charge-charge repulsion with negatively charged E175. Quaternary structure appears closest to that of the wild-type enzyme
R138A
activity is approximately 0.1% of wild-type activity, Km-value for L-aspartate 4-semialdehyde is significantly higher than the wild-type value, shows the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
R138H
activity is approximately 0.1% of wild-type activity, Km-value for L-aspartate 4-semialdehyde is significantly higher than the wild-type value, shows the same IC50 values as the wild-type enzyme, but different partial inhibition patterns
T44S
the active site is intact, returns much but not all activity likely due to the flexibility of Ser44. Increased flexibility in the active site, which appears to facilitate the binding/reaction of substrate analogues
T44V
site-directed mutagenesis, reduced activity, structure is similar to the wild-type enzyme
Y107W
mutant, site-directed mutagenesis
Y133F
site-directed mutagenesis, reduced activity, structure is similar to the wild-type enzyme
A49K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
A49P
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme and is still sensitive to L-lysine
A49W
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E84T
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme and is insensitive to L-lysine
H56K
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme and is insensitive to L-lysine
L197D/Y107W
-
site-directed mutagenesis, the mutant forms a monomer that is catalytically active, but with reduced catalytic efficiency, displaying 8% of the specific activity of the wild-type enzyme. The Michaelis constants for the substrates pyruvate and for (S)-aspartate semialdehyde increase by an order of magnitude. L197D/Y107W is expressed as a folded monomer
L51K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
L51T
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme and is sill sensitive to L-lysine
K161A
catalytically active, significant decrease in activity. Is not inactivated when incubated with pyruvate and the reducing agent sodium borohydride. Negligible heat production associated with pyruvate binding to the mutant enzyme, consistent with the lack of Schiff base formation
K161A
substantially diminished binding affinity of pyruvate, the surrounding active site scaffold is unable to compensate the entropic penalty associated with ligand localisation in the absence of Schiff-base formation
Y107F
site-directed mutagenesis, reduced activity, structure is similar to the wild-type enzyme
Y107F
mutant, site-directed mutagenesis
additional information
detailed structural properties of the mutant enzymes based on the crystal structure models
additional information
-
detailed structural properties of the mutant enzymes based on the crystal structure models
additional information
C-terminal truncated DHDPS (H225*), exhibits a dramatic reduction in both solubility and stability. Equilibrating mixture of quaternary states. The substrate, pyruvate, and the feedback inhibitor, (S)-lysine, both have a positive effect on thermostability of C-terminal truncated DHDPS (H225*)
additional information
-
C-terminal truncated DHDPS (H225*), exhibits a dramatic reduction in both solubility and stability. Equilibrating mixture of quaternary states. The substrate, pyruvate, and the feedback inhibitor, (S)-lysine, both have a positive effect on thermostability of C-terminal truncated DHDPS (H225*)
additional information
-
disruption of quaternary structure of DHDPS generates a functional monomer that is no longer inhibited by lysine, overview
additional information
-
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
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