EC Number |
Reference |
---|
1.14.13.242 | - |
439054, 654133, 696331 |
1.14.13.242 | crystal structure analysis, PDB ID 5hxi, comparison to the structure of HbpA from Pseudomonas nitroreducens strain HBP1 (PDB ID 4cy8) |
763846 |
1.14.13.242 | 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 |
725780 |
1.14.13.242 | hanging drop vapor diffusion method, using 8% (w/v) PEG 8000, 0.1 M Tris-HCl, pH 8.5 |
742939 |
1.14.13.242 | 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 |
763837 |
1.14.13.242 | 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 |
742939 |