4.3.3.7 additional information - - 33902, 33905, 33907, 33908, 33911, 33915, 664244 4.3.3.7 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 691786 4.3.3.7 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 690266 4.3.3.7 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 690252 4.3.3.7 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 701513 4.3.3.7 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 693141 4.3.3.7 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 692356 4.3.3.7 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 695011 4.3.3.7 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 690914 4.3.3.7 additional information - specific activity relatively high even at 30°C, structural model reveals that the active site is well conserved 692255 4.3.3.7 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 690628 4.3.3.7 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 691243 4.3.3.7 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 690983 4.3.3.7 0.0034 - purified mutant T44V 652939 4.3.3.7 0.008 - purified mutant Y133F 652939 4.3.3.7 0.27 - purified mutant Y107F 652939 4.3.3.7 0.72 - crude extract of mutant T44S 702479 4.3.3.7 0.81 - crude extract 701550 4.3.3.7 1.11 - purified enzyme 649771 4.3.3.7 1.5 - purified enzyme, recombinant enzyme in the absence of the substrate pyruvate 701513 4.3.3.7 1.61 - 2fold purified enzyme 701550 4.3.3.7 1.81 - purified wild-type enzyme 652939 4.3.3.7 2 - crude extract, recombinant enzyme in the absence of the substrate pyruvate 701513 4.3.3.7 12 - crude extract, recombinant enzyme in the presence of the substrate pyruvate 701513 4.3.3.7 14.5 - purified recombinant mutant L51K, pH 8.0, temperature not specified in the publication 729062 4.3.3.7 14.52 - 20.7fold purified mutant T44S 702479 4.3.3.7 19.2 - purified recombinant mutant A49K, pH 8.0, temperature not specified in the publication 729062 4.3.3.7 33 - purified enzyme, recombinant enzyme in the presence of the substrate pyruvate 701513 4.3.3.7 60.5 - purified recombinant mutant L51T, pH 8.0, temperature not specified in the publication 729062 4.3.3.7 75.6 - pH 8.0, 30°C, untagged enzyme 749225 4.3.3.7 81.6 - purified recombinant mutant A49W, pH 8.0, temperature not specified in the publication 729062 4.3.3.7 100 - - 33909 4.3.3.7 104 - purified recombinant His-tagged enzyme, pH not specified in the publication, temperature not specified in the publication 713631 4.3.3.7 112 - pH 8.0, 30°C, His-tagged enzyme 749225 4.3.3.7 174 - purified recombinant His-tagged enzyme, coupled assay, pH and temperature not specified in the publication 728891 4.3.3.7 454.2 - purified recombinant mutant H56K, pH 8.0, temperature not specified in the publication 729062 4.3.3.7 458 - - 33906 4.3.3.7 478.1 - purified recombinant mutant E84T, pH 8.0, temperature not specified in the publication 729062 4.3.3.7 500.8 - purified recombinant wild-type enzyme, pH 8.0, temperature not specified in the publication 729062 4.3.3.7 559.4 - purified recombinant mutant A49P, pH 8.0, temperature not specified in the publication 729062