Literature summary for 1.14.13.242 extracted from

Tian, B.; Strid, A.; Eriksson, L.A.
Catalytic roles of active-site residues in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: an ONIOM/DFT study (2011), J. Phys. Chem. B, 115, 1918-1926.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Mesorhizobium loti

Crystallization (Comment)

Organism

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

Mesorhizobium loti

Organism

Organism	UniProt	Comment	Textmining
Mesorhizobium loti	-	-	-
Mesorhizobium loti MAFF303099	-	-	-

Synonyms

Synonyms	Comment	Organism
mlr6788	locus name	Mesorhizobium loti

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Release 2023.1 (January 2023)