Deciphering magnesium binding site and structure-function insights in a class II sesquiterpene cyclase.
Methods Enzymol
; 699: 25-57, 2024.
Article
en En
| MEDLINE
| ID: mdl-38942506
ABSTRACT
Magnesium ions (Mg2+) are crucial in class II terpene cyclases that utilize substrates with diphosphate groups. Interestingly, these enzymes catalyze reactions without cleaving the diphosphate group, instead initiating the reaction through protonation. In our recent research, we discovered a novel class II sesquiterpene cyclase in Streptomyces showdoensis. Notably, we determined its crystal structure and identified Mg2+ within its active site. This finding has shed light on the previously elusive question of Mg2+ binding in class II terpene cyclases. In this chapter, we outline our methods for discovering this novel enzyme, including steps for its purification, crystallization, and kinetic analysis.
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1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Sesquiterpenos
/
Streptomyces
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Magnesio
Idioma:
En
Revista:
Methods Enzymol
Año:
2024
Tipo del documento:
Article