Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 85
Volume 85, Issue -, Pages 485-514Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-060713-035504
Keywords
iron-sulfur cluster; molybdenum cofactor; lipoic acid; tRNA modifications; Elongator; S-adenosylmethionine; radicals; viperin
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Funding
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R21AI111419] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM103268, R01GM101957] Funding Source: NIH RePORTER
- NIAID NIH HHS [R21 AI111419] Funding Source: Medline
- NIGMS NIH HHS [R01 GM103268, R01 GM101957] Funding Source: Medline
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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.
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