Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | mononuclear non-heme iron enzyme | Pseudomonas putida |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,5-dihydroxypyridine + O2 | Pseudomonas putida | - |
N-formylmaleamic acid | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | Q88FY1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,5-dihydroxypyridine + O2 | - |
Pseudomonas putida | N-formylmaleamic acid | - |
? | |
2,5-dihydroxypyridine + O2 | a series of combined quantum mechanics and molecular mechanics (QM/MM) calculations is performed to illuminate the catalytic mechanism of 2,5-dihydroxypyridine dioxygenase (NicX). On the basis of the calculations, the most plausible reaction pathway and the structures of transition states and intermediates involved in the reaction, as well as the energy profiles, are described in detail | Pseudomonas putida | N-formylmaleamic acid | - |
? | |
2,5-dihydroxypyridine + O2 | two key factors may influence the substrate specificity of the enzyme (NicX): 1. the successful binding of substrates in the active center, in which the pocket residues, including His189, His105, and Glu177, play a key role in substrate recognition, 2. the activation of the substrate by electron transfer from the substrate to dioxygen. Based on the crystal structure of the 2,5-dihydroxypyridine dioxygenase (NicX), an enzyme-substrate complex model is constructed and QM/MM calculations are carried out to unravel the mechanism of NicX-catalyzed heterocyclic ring cleavage involved in the biochemical degradation of nicotine | Pseudomonas putida | N-formylmaleamic acid | - |
? |
Synonyms | Comment | Organism |
---|---|---|
2,5-dihydroxypyridine dioxygenase | - |
Pseudomonas putida |
NicX | - |
Pseudomonas putida |