Radical S-Adenosylmethionine Enzymes in Human Health and Disease

Bradley J. Landgraf, Erin L. McCarthy, Squire J. Booker

Research output: Contribution to journalArticle

62 Citations (Scopus)

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-N6-isopentenyladenosine biosynthesis; CDKAL1, methylthio-N6-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.

Original languageEnglish (US)
Pages (from-to)485-514
Number of pages30
JournalAnnual Review of Biochemistry
Volume85
DOIs
StatePublished - Jun 2 2016

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S-Adenosylmethionine
Biosynthesis
Health
Isopentenyladenosine
Enzymes
Thioctic Acid
Uridine
Gene encoding
Mutation
Aberrations
Proteins

All Science Journal Classification (ASJC) codes

  • Medicine(all)
  • Biochemistry

Cite this

Landgraf, Bradley J. ; McCarthy, Erin L. ; Booker, Squire J. / Radical S-Adenosylmethionine Enzymes in Human Health and Disease. In: Annual Review of Biochemistry. 2016 ; Vol. 85. pp. 485-514.
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Radical S-Adenosylmethionine Enzymes in Human Health and Disease. / Landgraf, Bradley J.; McCarthy, Erin L.; Booker, Squire J.

In: Annual Review of Biochemistry, Vol. 85, 02.06.2016, p. 485-514.

Research output: Contribution to journalArticle

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