Enzymes of the crotonase superfamily: Diverse assembly and diverse function.
Curr Opin Struct Biol
; 82: 102671, 2023 10.
Article
en En
| MEDLINE
| ID: mdl-37542911
ABSTRACT
The crotonase fold is generated by a framework of four repeats of a ßßα-unit, extended by two helical regions. The active site of crotonase superfamily (CS) enzymes is located at the N-terminal end of the helix of the third repeat, typically being covered by a C-terminal helix. A major subset of CS-enzymes catalyzes acyl-CoA-dependent reactions, allowing for a diverse range of acyl-tail modifications. Most of these enzymes occur as trimers or hexamers (dimers of trimers), but monomeric forms are also observed. A common feature of the active sites of CS-enzymes is an oxyanion hole, formed by two peptide-NH hydrogen bond donors, which stabilises the negatively charged thioester oxygen atom of the reaction intermediate. Structural properties and possible use of these enzymes for biotechnological applications are discussed.
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Acilcoenzima A
/
Enoil-CoA Hidratasa
Idioma:
En
Revista:
Curr Opin Struct Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2023
Tipo del documento:
Article
País de afiliación:
Finlandia