Role of Key Residues at the Flavin Mononucleotide (FMN):Adenylyltransferase Catalytic Site of the Bifunctional Riboflavin Kinase/Flavin Adenine Dinucleotide (FAD)  Synthetase from Corynebacterium ammoniagenes

Role of Key Residues at the Flavin Mononucleotide (FMN):Adenylyltransferase Catalytic Site of the Bifunctional Riboflavin Kinase/Flavin Adenine Dinucleotide (FAD)  Synthetase from Corynebacterium ammoniagenes

In mammals and in yeast the conversion of Riboflavin (RF) into flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) is catalysed by the sequential action of two enzymes: an ATP:riboflavin kinase (RFK) and an ATP:FMN adenylyltransferase (FMNAT). However, most prokaryotes depend on a sing...

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Bibliographic Details
Main Authors: Susana Frago, Adrián Velázquez-Campoy, Milagros Medina, Ana Serrano
Format: Article
Language:English
Published: MDPI AG 2012-11-01
Series:International Journal of Molecular Sciences
Subjects:
FAD synthetase
ATP:riboflavin kinase
ATP:FMN adenylyltransferase
FAD pyrophosphorylase
site-directed mutagenesis
catalytic activity
substrate binding
Online Access:http://www.mdpi.com/1422-0067/13/11/14492

Internet

http://www.mdpi.com/1422-0067/13/11/14492

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