In vitro kinetic study of the squalestatin tetraketide synthase dehydratase reveals the stereochemical course of a fungal highly reducing polyketide synthase.
Chem Commun (Camb)
; 53(10): 1727-1730, 2017 Feb 04.
Article
en En
| MEDLINE
| ID: mdl-28106181
ABSTRACT
Six potential diketide substrates for the squalestatin tetraketide synthase (SQTKS) dehydratase (DH) domain were synthesised as N-acetyl cysteamine thiolesters (SNAC) and tested in kinetic assays as substrates with an isolated DH domain. 3R-3-hydroxybutyryl SNAC 3R-16 was turned over by the enzyme, but its enantiomer was not. Of the four 2-methyl substrates only 2R,3R-2-methyl-3-hydroxybutyryl SNAC 2R,3R-8 was a substrate. Combined with stereochemical information from the isolated SQTKS enoyl reductase (ER) domain, our results provide a near complete stereochemical description of the first cycle of beta-modification reactions of a fungal highly reducing polyketide synthase (HR-PKS). The results emphasise the close relationship between fungal HR-PKS and vertebrate fatty acid synthases (vFAS).
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Banco de datos:
MEDLINE
Asunto principal:
Ácidos Tricarboxílicos
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Compuestos Bicíclicos Heterocíclicos con Puentes
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Ciclohexanonas
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Sintasas Poliquetidas
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Disacáridos
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Hongos
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Hidroliasas
Idioma:
En
Año:
2017
Tipo del documento:
Article