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Structure of 4-pyridoxolactonase from Mesorhizobium loti.

ABSTRACT: 4-Pyridoxolactonase from Mesorhizobium loti catalyzes the zinc-dependent lactone-ring hydrolysis of 4-pyridoxolactone (4PAL) to 4-pyridoxic acid (4PA) in vitamin B6 degradation pathway I. The crystal structures of 4-pyridoxolactonase and its complex with 5-pyridoxolactone (5PAL; the competitive inhibitor) were determined. The overall structure was an ??/?? sandwich fold, and two zinc ions were coordinated. This strongly suggested that the enzyme belongs to subclass B3 of the class B ?-lactamases. In the complex structure, the carbonyl group of 5PAL pointed away from the active site, revealing why it acts as a competitive inhibitor. Based on docking simulation with 4PAL, 4PA and a reaction intermediate, 4-pyridoxolactonase probably catalyzes the reaction through a subclass B2-like mechanism, not the subclass B3 mechanism.

SUBMITTER: Kobayashi J

PROVIDER: S-EPMC3976056 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Structure of 4-pyridoxolactonase from Mesorhizobium loti.

Kobayashi Jun J Yoshikane Yu Y Yagi Toshiharu T Baba Seiki S Mizutani Kimihiko K Takahashi Nobuyuki N Mikami Bunzo B

Acta crystallographica. Section F, Structural biology communications 20140325 Pt 4

4-Pyridoxolactonase from Mesorhizobium loti catalyzes the zinc-dependent lactone-ring hydrolysis of 4-pyridoxolactone (4PAL) to 4-pyridoxic acid (4PA) in vitamin B6 degradation pathway I. The crystal structures of 4-pyridoxolactonase and its complex with 5-pyridoxolactone (5PAL; the competitive inhibitor) were determined. The overall structure was an αβ/βα sandwich fold, and two zinc ions were coordinated. This strongly suggested that the enzyme belongs to subclass B3 of the class B β-lactamases ...[more]

PMID: 24699732

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