| Literature DB >> 27145839 |
Bradley J Landgraf1, Erin L McCarthy2, Squire J Booker1,2,3.
Abstract
Radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Of approximately 114,000 of these enzymes, 8 are known to be present in humans: MOCS1, molybdenum cofactor biosynthesis; LIAS, lipoic acid biosynthesis; CDK5RAP1, 2-methylthio-N(6)-isopentenyladenosine biosynthesis; CDKAL1, methylthio-N(6)-threonylcarbamoyladenosine biosynthesis; TYW1, wybutosine biosynthesis; ELP3, 5-methoxycarbonylmethyl uridine; and RSAD1 and viperin, both of unknown function. Aberrations in the genes encoding these proteins result in a variety of diseases. In this review, we summarize the biochemical characterization of these 8 radical S-adenosylmethionine enzymes and, in the context of human health, describe the deleterious effects that result from such genetic mutations.Entities:
Keywords: Elongator; S-adenosylmethionine; iron–sulfur cluster; lipoic acid; molybdenum cofactor; radicals; tRNA modifications; viperin
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Year: 2016 PMID: 27145839 DOI: 10.1146/annurev-biochem-060713-035504
Source DB: PubMed Journal: Annu Rev Biochem ISSN: 0066-4154 Impact factor: 23.643