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Results 1 - 7 of 7
EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the reaction diagram Show all sequences 3.5.1.107maleamate + H2O - Pseudomonas putida maleate + NH3 - ?
Display the reaction diagram Show all sequences 3.5.1.107maleamate + H2O - Bordetella bronchiseptica maleate + NH3 - ?
Display the reaction diagram Show all sequences 3.5.1.107maleamate + H2O aerobic catabolism of nicotinic acid Pseudomonas putida maleate + NH3 - ?
Display the reaction diagram Show all sequences 3.5.1.107maleamate + H2O multiscale computational enzymology is used to investigate the catalytic mechanism, substrate binding, oxyanion hole, and roles of key active site residues of the enzyme. Molecular dynamics (MD) simulations, quantum mechanics/molecular mechanics (QM/MM) and QTAIM methods are applied. The mechanism of the NicF-catalyzed reaction proceeds by a nucleophilic addition-elimination sequence involving the formation of a thioester enzyme intermediate (IC2 in stage 1) followed by hydrolysis of the thioester bond to form the products (stage 2). Consequently, the formation of IC2 in stage 1 is the rate-limiting step with a barrier of 88.8 kJ/mol relative to the reactant complex, RC. Along with -NH- donor groups of the oxyanion hole (i.e., HN-Thr146, HN-Cys150), the active site beta-hydroxyl of threonine (HO-betaThr146) is concluded to play a role in stabilizing the carbonyl oxygen of maleamate during the mechanism Bordetella bronchiseptica maleate + NH3 - ?
Display the reaction diagram Show all sequences 3.5.1.107maleamate + H2O - Bordetella bronchiseptica ATCC BAA-588 maleate + NH3 - ?
Display the reaction diagram Show all sequences 3.5.1.107maleamate + H2O multiscale computational enzymology is used to investigate the catalytic mechanism, substrate binding, oxyanion hole, and roles of key active site residues of the enzyme. Molecular dynamics (MD) simulations, quantum mechanics/molecular mechanics (QM/MM) and QTAIM methods are applied. The mechanism of the NicF-catalyzed reaction proceeds by a nucleophilic addition-elimination sequence involving the formation of a thioester enzyme intermediate (IC2 in stage 1) followed by hydrolysis of the thioester bond to form the products (stage 2). Consequently, the formation of IC2 in stage 1 is the rate-limiting step with a barrier of 88.8 kJ/mol relative to the reactant complex, RC. Along with -NH- donor groups of the oxyanion hole (i.e., HN-Thr146, HN-Cys150), the active site beta-hydroxyl of threonine (HO-betaThr146) is concluded to play a role in stabilizing the carbonyl oxygen of maleamate during the mechanism Bordetella bronchiseptica ATCC BAA-588 maleate + NH3 - ?
Display the reaction diagram Show all sequences 3.5.1.107maleamate + H2O - Bordetella bronchiseptica RB50 maleate + NH3 - ?
Results 1 - 7 of 7