An Iterative O-Methyltransferase Catalyzes 1,11-Dimethylation of Aspergillus fumigatus Fumaric Acid Amides.
Chembiochem
; 17(19): 1813-1817, 2016 10 04.
Article
en En
| MEDLINE
| ID: mdl-27442960
ABSTRACT
S-adenosyl-l-methionine (SAM)-dependent methyltransfer is a common biosynthetic strategy to modify natural products. We investigated the previously uncharacterized Aspergillus fumigatus methyltransferase FtpM, which is encoded next to the bimodular fumaric acid amide synthetase FtpA. Structure elucidation of two new A.â
fumigatus natural products, the 1,11-dimethyl esters of fumaryl-l-tyrosine and fumaryl-l-phenylalanine, together with ftpM gene disruption suggested that FtpM catalyzes iterative methylation. Final evidence that a single enzyme repeatedly acts on fumaric acid amides came from an in vitro biochemical investigation with recombinantly produced FtpM. Size-exclusion chromatography indicated that this methyltransferase is active as a dimer. As ftpA and ftpM homologues are found clustered in other fungi, we expect our work will help to identify and annotate natural product biosynthesis genes in various species.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Aspergillus fumigatus
/
Fumaratos
/
Amidas
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Metiltransferasas
Idioma:
En
Año:
2016
Tipo del documento:
Article