Specific Features for the Competent Binding of Substrates at the FMN Adenylyltransferase Site of FAD Synthase from <i>Corynebacterium ammoniagenes</i>
Bifunctional FAD synthases (FADSs) catalyze FMN (flavin mononucleotide) and FAD (flavinadenine dinucleotide) biosynthesis at their C-riboflavin kinase (RFK) and N-FMN:adenylyltransferase (FMNAT) modules, respectively. Biophysical properties and requirements for their FMNAT activity differ among spec...
Main Authors: | , , |
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Format: | Article |
Language: | English |
Published: |
MDPI AG
2019-10-01
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Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | https://www.mdpi.com/1422-0067/20/20/5083 |