Dissecting cobamide diversity through structural and functional analyses of the base-activating CobT enzyme of Salmonella enterica

• Published in: Biochimica et biophysica acta Vol. 1840; no. 1; pp. 464 - 475
• Main Authors: Chan, Chi Ho, Newmister, Sean A., Talyor, Keenan, Claas, Kathy R., Rayment, Ivan, Escalante-Semerena, Jorge C.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.01.2014
• Subjects: active sites; Amino Acid Sequence; B12 biosynthesis; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; benzimidazoles; Catalysis; catalytic activity; Catalytic Domain; Cobamide diversity; Cobamides - metabolism; Cresols - metabolism; crystal structure; Crystallography, X-Ray; Directed enzyme evolution; enzyme activity; enzymes; glutamic acid; Glutamic Acid - metabolism; in vivo studies; Kinetics; Lower base activation; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation - genetics; Nicotinamide Mononucleotide - analogs & derivatives; Nicotinamide Mononucleotide - metabolism; Nicotinamide Phosphoribosyltransferase - metabolism; Pentosyltransferases - chemistry; Pentosyltransferases - genetics; Pentosyltransferases - metabolism; phenolic compounds; Protein Conformation; purines; ribose; Salmonella enterica; Salmonella enterica - enzymology; Salmonella enterica - genetics; Salmonella enterica - growth & development; Sequence Homology, Amino Acid; site-directed mutagenesis; Substrate Specificity; B12 biosynthesis; Lower base activation; Cobamide diversity; Directed enzyme evolution; B biosynthesis

Cobamide diversity arises from the nature of the nucleotide base. Nicotinate mononucleotide (NaMN):base phosphoribosyltransferases (CobT) synthesize α-linked riboside monophosphates from diverse nucleotide base substrates (e.g., benzimidazoles, purines, phenolics) that are incorporated into cobamide...