3.5.1.107: maleamate amidohydrolase
This is an abbreviated version!
For detailed information about maleamate amidohydrolase, go to the full flat file.
Reaction
Synonyms
Bb1774, hpaF, NicF
ECTree
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Substrates Products
Substrates Products on EC 3.5.1.107 - maleamate amidohydrolase
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REACTION DIAGRAM
maleamate + H2O
maleate + NH3
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
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?
maleamate + H2O
maleate + NH3
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
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maleamate + H2O
maleate + NH3
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aerobic catabolism of nicotinic acid
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