Multi-domain terpenoid cyclase architecture and prospects for proximity in bifunctional catalysis.
Curr Opin Struct Biol
; 41: 27-37, 2016 12.
Article
em En
| MEDLINE
| ID: mdl-27285057
ABSTRACT
Crystal structures of terpenoid cyclases reveal assemblies of three basic domains designated α, ß, and γ. While the biosynthesis of cyclic monoterpenes (C10) and sesquiterpenes (C15) most often involves enzymes with α or αß domain architecture, the biosynthesis of cyclic diterpenes (C20), sesterterpenes (C25), and triterpenes (C30) can involve enzymes with α, αα, ßγ, or αßγ domain architecture. Indeed, some enzymes of terpenoid biosynthesis are bifunctional, with distinct active sites that catalyze sequential reactions. Interestingly, some of these enzymes oligomerize to form dimers, tetramers, and hexamers. Not only can such assemblies enable enzyme regulation by allostery, but they can also provide a modest enhancement of terpenoid product flux through proximity channeling or cluster channeling. The mixing and matching of functional terpenoid cyclase domains through tertiary and/or quaternary structure may also comprise an evolutionary strategy for facile product diversification.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Terpenos
/
Liases
Limite:
Humans
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article