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Annual Review of Biochemistry

Volume 85, 2016

Radical -Adenosylmethionine Enzymes in Human Health and Disease

Abstract

Radical -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-6-isopentenyladenosine biosynthesis; CDKAL1, methylthio-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 -adenosylmethionine enzymes and, in the context of human health, describe the deleterious effects that result from such genetic mutations.

Keyword(s): Elongator, iron–sulfur cluster, lipoic acid, molybdenum cofactor, radicals, S-adenosylmethionine, tRNA modifications, viperin
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2016-06-02
2024-04-18
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Radical S-Adenosylmethionine Enzymes in Human Health and Disease
Annual Review of Biochemistry 85, 485 (2016); https://doi.org/10.1146/annurev-biochem-060713-035504
/content/journals/10.1146/annurev-biochem-060713-035504
/content/journals/10.1146/annurev-biochem-060713-035504
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