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Results 1 - 10 of 40 > >>
EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Commentary Reference
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - - 33902, 33905, 33907, 33908, 33911, 33915, 664244
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - 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
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - 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
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - 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
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - 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
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - 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
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - 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
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - 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
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - 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
Show all pathways known for 4.3.3.7Display the word mapDisplay the reaction diagram Show all sequences 4.3.3.7-999 - specific activity relatively high even at 30°C, structural model reveals that the active site is well conserved 692255
Results 1 - 10 of 40 > >>