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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-dihydroxypyridine + O2 - Pseudomonas putida N-formylmaleamic acid - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-dihydroxypyridine + O2 - Cupriavidus campinensis N-formylmaleamic acid - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-dihydroxypyridine + O2 - Agrobacterium sp. DW-1 N-formylmaleamic acid - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-dihydroxypyridine + O2 activation with 10 mM DTT and 0.5 mM FeSO4 (25 min, 25°C) Pseudomonas putida N-formylmaleamic acid ring cleavage between carbon 5 and 6, further conversion to formic and maleamic acid is catalyzed by the NicD protein, a deformylase similar to some members of the alpha/beta-hydolase fold superfamily ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-dihydroxypyridine + O2 aerobic catabolism of nicotinic acid Pseudomonas putida N-formylmaleamic acid - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-dihydroxypyridine + O2 extradiol ring-cleavage dioxygenase cleaves between carbons 5 and 6 Pseudomonas putida N-formylmaleamic acid - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-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 - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-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 - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-dihydroxypyridine + O2 - Cupriavidus campinensis 23K8 N-formylmaleamic acid - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.92,5-dihydroxypyridine + O2 activation with 10 mM DTT and 0.5 mM FeSO4 (25 min, 25°C) Pseudomonas putida KT 2240 N-formylmaleamic acid ring cleavage between carbon 5 and 6, further conversion to formic and maleamic acid is catalyzed by the NicD protein, a deformylase similar to some members of the alpha/beta-hydolase fold superfamily ?
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