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 (Specific Activity
Specific Activity 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
SPECIFIC ACTIVITY [µmol/min/mg] 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1.5
Q81WN7
purified enzyme, recombinant enzyme in the absence of the substrate pyruvate
104
-
purified recombinant His-tagged enzyme, pH not specified in the publication, temperature not specified in the publication
12
Q81WN7
crude extract, recombinant enzyme in the presence of the substrate pyruvate
14.5
-
purified recombinant mutant L51K, pH 8.0, temperature not specified in the publication
174
purified recombinant His-tagged enzyme, coupled assay, pH and temperature not specified in the publication
19.2
-
purified recombinant mutant A49K, pH 8.0, temperature not specified in the publication
2
Q81WN7
crude extract, recombinant enzyme in the absence of the substrate pyruvate
33
Q81WN7
purified enzyme, recombinant enzyme in the presence of the substrate pyruvate
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
additional information
Q81WN7
DHDPS purified in the presence of pyruvate yields a greater amount of recombinant enzyme with 22fold greater specific activity compared with the enzyme purified in the absence of substrate
additional information
-
DHDPS purified in the presence of pyruvate yields a greater amount of recombinant enzyme with 22fold greater specific activity compared with the enzyme purified in the absence of substrate
additional information
specific activity relatively high even at 30°C, structural model reveals that the active site is well conserved
additional information
-
specific activity relatively high even at 30°C, structural model reveals that the active site is well conserved
additional information
structure in vicinity of the putative binding site for S-lysine indicates that the allosteric binding site in the Escherichia coli dihydrodipicolinate synthase does not exist in the enzyme of Corynebacterium glutamicum, difference of three non-conservative amino acids substitutions, explains lack of feedback inhibition by lysine in Corynebacterium glutamicum
additional information
-
structure in vicinity of the putative binding site for S-lysine indicates that the allosteric binding site in the Escherichia coli dihydrodipicolinate synthase does not exist in the enzyme of Corynebacterium glutamicum, difference of three non-conservative amino acids substitutions, explains lack of feedback inhibition by lysine in Corynebacterium glutamicum
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
analysis of ability of rhizopines to interact with MosA protein in the presence and absence of methyl donors, no methyltransferase activity observed in the presence of scyllo-inosamine and S-adenosylmethionine (SAM), presence of rhizopine compounds does not affect kinetics of dihydrodipicolinate synthesis
additional information
titration of (S)-lysine into buffered solutions of MosA protein in the presence or absence of saturating amounts of pyruvate, thermodynamic data for (S)-Lysine binding to MosA protein, non-competitive mechanism with substrate-dependent differences in the energetics of inhibitor binding
additional information
archetypal subunit orientation in the crystal structure of other dihydrodipicolinate synthase enzymes not observed, structure refinement will provide information regarding the structural evolution of dihydrodipicolinate synthase and the design of antibiotics targeting lysine biosynthesis in Staphylococcus aureus
additional information
-
archetypal subunit orientation in the crystal structure of other dihydrodipicolinate synthase enzymes not observed, structure refinement will provide information regarding the structural evolution of dihydrodipicolinate synthase and the design of antibiotics targeting lysine biosynthesis in Staphylococcus aureus
additional information
mechanistic insight into catalysis, structural features and the evolution of quarternary structure, MRSA-DHDPS enzyme exists in a monomer-dimer equilibrium in solution, MRSA-DHDPS dimer is catalytically active
additional information
-
mechanistic insight into catalysis, structural features and the evolution of quarternary structure, MRSA-DHDPS enzyme exists in a monomer-dimer equilibrium in solution, MRSA-DHDPS dimer is catalytically active
additional information
quaternary structure different from other characterized homologues, dimer both in solution and in the crystal, catalytically important Lys-163 and the proton relay catalytic triad comprising Thr-46, Tyr-109 and Tyr-135 corresponds well with the enzyme homologue of Escherichia coli, deletion mutant lacking the three helical domains reveals a significant reduction in enzymatic activity, changes in the catalytic site upon pyruvate binding provide a structural basis for the ping-pong reaction mechanism, no feedback inhibition by lysine, free and substrate bound forms provide a structural rationale for catalytic mechanism, unique conformational features crucial for the design of specific non-competitive inhibitors
additional information
-
quaternary structure different from other characterized homologues, dimer both in solution and in the crystal, catalytically important Lys-163 and the proton relay catalytic triad comprising Thr-46, Tyr-109 and Tyr-135 corresponds well with the enzyme homologue of Escherichia coli, deletion mutant lacking the three helical domains reveals a significant reduction in enzymatic activity, changes in the catalytic site upon pyruvate binding provide a structural basis for the ping-pong reaction mechanism, no feedback inhibition by lysine, free and substrate bound forms provide a structural rationale for catalytic mechanism, unique conformational features crucial for the design of specific non-competitive inhibitors
