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1.14.13.242: 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase

This is an abbreviated version!
For detailed information about 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.242

Reaction

3-Hydroxy-2-methylpyridine-5-carboxylate
+
NAD(P)H
 +
H+
 +
O2
=
2-(acetamidomethylidene)succinate
 +
NAD(P)+

Synonyms

2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase, 2-methyl-3-hydroxypyridine 5-carboxylic acid oxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase, 3-hydroxy-2-methylpyridine carboxylate dioxygenase, 3-hydroxy-2-methylpyridinecarboxylate dioxygenase, EC 1.14.12.4, methylhydroxypyridine carboxylate dioxygenase, methylhydroxypyridinecarboxylate oxidase, MHPCO, mlr6788

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.242 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase

Crystallization

Crystallization on EC 1.14.13.242 - 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, PDB ID 5hxi, comparison to the structure of HbpA from Pseudomonas nitroreducens strain HBP1 (PDB ID 4cy8)
structure in complex with FAD. Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida, EC 1.14.13.2, 2-hydroxybiphenyl 3-monooxygenase (HbpA) from Pseudomonas nitroreducens, EC 1.14.13.44, and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum. The portions of the residues required for substrate and FAD binding are identical, including the betaalphabeta fold and beta-sheet wall
density functional theory/molecular mechanics calculations show that the active-site residues Arg211 and Tyr223 have a minor effect on the reaction, while the peptide bond of Pro295-Ala296, the side chain of Tyr82 and several crystal water molecules affect the reaction energy profile considerably. The ring-opening pathway, in which an epoxy transition state is formed, is more favored than the direct C2-C3 cleavage pathway. Both the reaction barriers for the hydroxylation and the ring-opening pathways are sensitive to the quantum mechanics/molecular mechanics partitioning
-
hanging drop vapor diffusion method, using 8% (w/v) PEG 8000, 0.1 M Tris-HCl, pH 8.5
structure of enzyme with and without substrates 2-methyl-3-hydroxypyridine-5-carboxylic acid, 5-hydroxynicotinic acid and 5-pyridoxic acid, and of mutant Y270F. Residue Y270 is located in the active site