[HTML][HTML] Diversity of the reaction mechanisms of SAM-dependent enzymes
Q Sun, M Huang, Y Wei - Acta Pharmaceutica Sinica B, 2021 - Elsevier
S-adenosylmethionine (SAM) is ubiquitous in living organisms and is of great significance in
metabolism as a cofactor of various enzymes. Methyltransferases (MTases), a major group …
metabolism as a cofactor of various enzymes. Methyltransferases (MTases), a major group …
Radical SAM enzymes in the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs)
A Benjdia, C Balty, O Berteau - Frontiers in chemistry, 2017 - frontiersin.org
Ribosomally-synthesized and post-translationally modified peptides (RiPPs) are a large and
diverse family of natural products. They possess interesting biological properties such as …
diverse family of natural products. They possess interesting biological properties such as …
Reaction Catalyzed by GenK, a Cobalamin-Dependent Radical S-Adenosyl-l-methionine Methyltransferase in the Biosynthetic Pathway of Gentamicin, Proceeds …
Many cobalamin (Cbl)-dependent radical S-adenosyl-l-methionine (SAM)
methyltransferases have been identified through sequence alignment and/or genetic …
methyltransferases have been identified through sequence alignment and/or genetic …
Accessing and exploring the unusual chemistry by radical SAM-RiPP enzymes
Q Guo, BI Morinaka - Current Opinion in Chemical Biology, 2024 - Elsevier
Radical SAM enzymes involved in the biosynthesis of ribosomally synthesized and post-
translationally modified peptides catalyze unusual transformations that lead to unique …
translationally modified peptides catalyze unusual transformations that lead to unique …
Cobalamin-dependent radical S-adenosyl-l-methionine enzymes in natural product biosynthesis
SC Wang - Natural product reports, 2018 - pubs.rsc.org
Covering: 2011 to 2018 This highlight summarizes the investigation of cobalamin (Cbl)-and
radical S-adenosyl-L-methionine (SAM)-dependent enzymes found in natural product …
radical S-adenosyl-L-methionine (SAM)-dependent enzymes found in natural product …
Watasemycin biosynthesis in Streptomyces venezuelae: thiazoline C-methylation by a type B radical-SAM methylase homologue
2-Hydroxyphenylthiazolines are a family of iron-chelating nonribosomal peptide natural
products that function as virulence-conferring siderophores in various Gram-negative …
products that function as virulence-conferring siderophores in various Gram-negative …
Stereospecific Radical-Mediated B12-Dependent Methyl Transfer by the Fosfomycin Biosynthesis Enzyme Fom3
MI McLaughlin, WA Van Der Donk - Biochemistry, 2018 - ACS Publications
Fom3, the antepenultimate enzyme in the fosfomycin biosynthetic pathway in Streptomyces
spp., is a class B cobalamin-dependent radical SAM methyltransferase that catalyzes …
spp., is a class B cobalamin-dependent radical SAM methyltransferase that catalyzes …
Functional diversity of HemN-like proteins
J Cheng, WQ Liu, X Zhu, Q Zhang - ACS bio & med Chem Au, 2022 - ACS Publications
HemN is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the anaerobic
oxidative decarboxylation of coproporphyrinogen III to produce protoporphyrinogen IX, a key …
oxidative decarboxylation of coproporphyrinogen III to produce protoporphyrinogen IX, a key …
Methylations in complex carbapenem biosynthesis are catalyzed by a single cobalamin-dependent radical S-adenosylmethionine enzyme
EK Sinner, MS Lichstrahl, R Li, DR Marous… - Chemical …, 2019 - pubs.rsc.org
Complex carbapenem β-lactam antibiotics contain diverse C6 alkyl substituents constructed
by cobalamin-dependent radical SAM enzymes. TokK installs the C6 isopropyl chain found …
by cobalamin-dependent radical SAM enzymes. TokK installs the C6 isopropyl chain found …
The Catalytic Mechanism of the Class C Radical S‐Adenosylmethionine Methyltransferase NosN
S‐Adenosylmethionine (SAM) is one of the most common co‐substrates in enzyme‐
catalyzed methylation reactions. Most SAM‐dependent reactions proceed through an SN2 …
catalyzed methylation reactions. Most SAM‐dependent reactions proceed through an SN2 …