Evolution of NAD biosynthetic enzymes
- PMID: 16154080
- DOI: 10.1016/j.str.2005.08.004
Evolution of NAD biosynthetic enzymes
Abstract
Two research groups have solved crystal structures of nicotinic acid phosphoribosyltransferase (PRTase) and made the argument that PRTases in three distinct pathways of nicotinamide adenine dinucleotide (NAD) biosynthesis evolved from a common ancestor (Shin et al., 2005 and Chappie et al., 2005).
Comment on
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Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum.J Biol Chem. 2005 May 6;280(18):18326-35. doi: 10.1074/jbc.M501622200. Epub 2005 Mar 6. J Biol Chem. 2005. PMID: 15753098
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The structure of a eukaryotic nicotinic acid phosphoribosyltransferase reveals structural heterogeneity among type II PRTases.Structure. 2005 Sep;13(9):1385-96. doi: 10.1016/j.str.2005.05.016. Structure. 2005. PMID: 16154095
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