EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.107 | additional information | metal-dependent enzyme | Bordetella bronchiseptica |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.107 | maleamate + H2O | Bordetella bronchiseptica | - |
maleate + NH3 | - |
? | |
3.5.1.107 | maleamate + H2O | Bordetella bronchiseptica ATCC BAA-588 | - |
maleate + NH3 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.107 | Bordetella bronchiseptica | A0A0H3LKK8 | - |
- |
3.5.1.107 | Bordetella bronchiseptica ATCC BAA-588 | A0A0H3LKK8 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.107 | maleamate + H2O | - |
Bordetella bronchiseptica | maleate + NH3 | - |
? | |
3.5.1.107 | maleamate + 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 | - |
? | |
3.5.1.107 | maleamate + H2O | - |
Bordetella bronchiseptica ATCC BAA-588 | maleate + NH3 | - |
? | |
3.5.1.107 | maleamate + 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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.107 | NicF | - |
Bordetella bronchiseptica |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.107 | metabolism | key enzyme in vitamin B3 metabolism | Bordetella bronchiseptica |