1.13.11.48: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
This is an abbreviated version!
For detailed information about 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase, go to the full flat file.
Reaction
Synonyms
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase, 1H-3-hydroxy-4-oxoquinaldine oxygenase, 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase, HOD, HodC, More
ECTree
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Reaction
Reaction on EC 1.13.11.48 - 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
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catalytic mechanism, overview. H251 acts as a general base to abstract a proton from the organic substrate. Residue S101, which corresponds to the nucleophile of the catalytic triad of alpha/beta-hydrolases, presumably participates in binding the heteroaromatic substrate. H102 and residues located in the topological region of the triad's acidic residue appear to influence O2 binding and reactivity. Role of Y196 of Hod as hydrogen-bondforming residue to oxygen atoms or even proton donor to negative charges of catalytic intermediates
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
catalytic mechanism, overview. H251 acts as a general base to abstract a proton from the organic substrate. Residue S101, which corresponds to the nucleophile of the catalytic triad of alpha/beta-hydrolases, presumably participates in binding the heteroaromatic substrate. H102 and residues located in the topological region of the triad's acidic residue appear to influence O2 binding and reactivity. Role of Y196 of Hod as hydrogen-bondforming residue to oxygen atoms or even proton donor to negative charges of catalytic intermediates
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3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
catalytic mechanism, overview. H251 acts as a general base to abstract a proton from the organic substrate. Residue S101, which corresponds to the nucleophile of the catalytic triad of alpha/beta-hydrolases, presumably participates in binding the heteroaromatic substrate. H102 and residues located in the topological region of the triad's acidic residue appear to influence O2 binding and reactivity. Role of Y196 of Hod as hydrogen-bondforming residue to oxygen atoms or even proton donor to negative charges of catalytic intermediates
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