Structure of methyltransferase RedM that forms the dimethylpyrrolinium of the bisindole reductasporine.

Daniel-Ivad, Phillip; Ryan, Katherine S

Daniel-Ivad, Phillip; Ryan, Katherine S.

Affiliation

Daniel-Ivad P; Department of Chemistry, The University of British Columbia, Vancouver, Canada.
Ryan KS; Department of Chemistry, The University of British Columbia, Vancouver, Canada. Electronic address: ksryan@chem.ubc.ca.

J Biol Chem ; 300(1): 105520, 2024 Jan.

Article in En | MEDLINE | ID: mdl-38042494

Subject(s)

Biological Products; Methyltransferases; Methyltransferases/genetics; Escherichia coli/genetics; Escherichia coli/metabolism; Oxidoreductases/chemistry; Mutagenesis, Site-Directed; Biological Products/metabolism; Catalysis; Crystallography, X-Ray

Key words

biosynthesis; crystal structure; enzyme catalysis; indolocarbazole; methyltransferase; site-directed mutagenesis

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Biological Products / Methyltransferases Language: En Journal: J Biol Chem Year: 2024 Type: Article Affiliation country: Canada

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