Radical S-Adenosylmethionine Enzymes

JB Broderick, BR Duffus, KS Duschene… - Chemical …, 2014 - ACS Publications
It was once widely held that nearly all reactions in biology were catalyzed via mechanisms
involving paired electron species. Beginning approximately 40 years ago, this paradigm was …

The mononuclear molybdenum enzymes

R Hille, J Hall, P Basu - Chemical reviews, 2014 - ACS Publications
Molybdenum is the only second-row transition metal required by most living organisms, and
is nearly universally distributed in biology. Enzymes containing molybdenum in their active …

The molybdenum cofactor

RR Mendel - Journal of Biological Chemistry, 2013 - ASBMB
The transition element molybdenum needs to be complexed by a special cofactor to gain
catalytic activity. Molybdenum is bound to a unique pterin, thus forming the molybdenum …

Radical S-Adenosylmethionine Enzymes in Human Health and Disease

BJ Landgraf, EL McCarthy… - Annual review of …, 2016 - annualreviews.org
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 …

SPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymes

TAJ Grell, PJ Goldman, CL Drennan - Journal of Biological Chemistry, 2015 - ASBMB
S-Adenosylmethionine (SAM, also known as AdoMet) radical enzymes use SAM and a [4Fe-
4S] cluster to catalyze a diverse array of reactions. They adopt a partial triose-phosphate …

Molybdenum cofactor and human disease

G Schwarz - Current opinion in chemical biology, 2016 - Elsevier
Highlights•Molybdenum cofactor is required in two mitochondrial and two cytosolic human
enzymes.•Molybdenum enzymes are able to reduce nitrite to nitric oxide (NO).•Deficiency of …

C–C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products

K Yokoyama, EA Lilla - Natural product reports, 2018 - pubs.rsc.org
Covering: up to the end of 2017 C–C bond formations are frequently the key steps in
cofactor and natural product biosynthesis. Historically, C–C bond formations were thought to …

[HTML][HTML] Auxiliary iron–sulfur cofactors in radical SAM enzymes

ND Lanz, SJ Booker - Biochimica et Biophysica Acta (BBA)-Molecular Cell …, 2015 - Elsevier
A vast number of enzymes are now known to belong to a superfamily known as radical SAM,
which all contain a [4Fe–4S] cluster ligated by three cysteine residues. The remaining …

X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification

PJ Goldman, TL Grove, LA Sites… - Proceedings of the …, 2013 - National Acad Sciences
Arylsulfatases require a maturating enzyme to perform a co-or posttranslational modification
to form a catalytically essential formylglycine (FGly) residue. In organisms that live …

Radical S-adenosylmethionine enzyme catalyzed thioether bond formation in sactipeptide biosynthesis

L Flühe, MA Marahiel - Current opinion in chemical biology, 2013 - Elsevier
Highlights•Sactipeptides represent a new class of ribosomally and postranslationally
modified peptides.•Characteristics of sactipeptides: thioether bond, bridging the S of a …