Literature summary for 3.1.8.1 extracted from

Ben-David, M.; Elias, M.; Filippi, J.J.; Dunach, E.; Silman, I.; Sussman, J.L.; Tawfik, D.S.
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1 (2012), J. Mol. Biol., 418, 181-196.

Crystallization (Commentary)

Crystallization (Comment)	Organism
protein at pH 6.5 and in complex with 2-hydroxyquinoline. The models suggest that promiscuity is driven by coincidental overlaps between the reactive intermediate for the native lactonase reaction and the ground and/or intermediate states of the promiscuous reactions. This overlap is also enabled by different active-site conformations: the lactonase activity utilizes one active-site conformation whereas the promiscuous phosphotriesterase activity utilizes another	synthetic construct

Crystallization (Comment)

Organism

protein at pH 6.5 and in complex with 2-hydroxyquinoline. The models suggest that promiscuity is driven by coincidental overlaps between the reactive intermediate for the native lactonase reaction and the ground and/or intermediate states of the promiscuous reactions. This overlap is also enabled by different active-site conformations: the lactonase activity utilizes one active-site conformation whereas the promiscuous phosphotriesterase activity utilizes another

synthetic construct

Organism

Organism	UniProt	Comment	Textmining
synthetic construct	-	-	-

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Release 2023.1 (January 2023)