Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217.
@article{Allen2014SpectroscopicCA, title={Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217.}, author={Kylie D. Allen and Susan C Wang}, journal={Biochimica et biophysica acta}, year={2014}, volume={1844 12}, pages={ 2135-44 } }
23 Citations
Reaction Catalyzed by GenK, a Cobalamin-Dependent Radical S-Adenosyl-l-methionine Methyltransferase in the Biosynthetic Pathway of Gentamicin, Proceeds with Retention of Configuration.
- Biology, ChemistryJournal of the American Chemical Society
- 2017
A model of GenK catalysis is proposed wherein free rotation of the radical-bearing carbon is prevented and the radical SAM machinery sits adjacent rather than opposite to the Me-Cbl cofactor with respect to the substrate in the enzyme active site.
The B12-Radical SAM Enzyme PoyC Catalyzes Valine Cβ-Methylation during Polytheonamide Biosynthesis
- Biology, ChemistryJournal of the American Chemical Society
- 2016
In vitro activity of PoyC is reported, the first B12-dependent rSAM enzyme catalyzing peptide Cβ-methylation, and it is demonstrated for the first time that B 12-rSAM enzymes have a tightly bound MeCbl cofactor that during catalysis transfers a methyl group originating from S-adenosyl-l-methionine.
Studies of GenK and OxsB, two B12-dependent radical SAM enzymes involved in natural product biosynthesis
- BiologyMethods in Enzymology
- 2022
Biosynthesis of Oxetanocin-A Includes a B12-Dependent Radical SAM Enzyme That Can Catalyze both Oxidative Ring Contraction and the Demethylation of SAM.
- Chemistry, BiologyBiochemistry
- 2021
Experiments reported herein reveal that OxsB/OxsA complex formation is crucial for the ring contraction reaction and that reduction of the aldehyde intermediate is catalyzed by a nonspecific dehydrogenase from the general cellular pool.
Analysis of Electrochemical Properties of S-Adenosyl-l-methionine and Implications for Its Role in Radical SAM Enzymes
- ChemistryJournal of the American Chemical Society
- 2019
The solution peak potential of SAM is measured to be ∼−1.4 V (v SHE) and it is shown that under controlled potential conditions, it undergoes irreversible fragmentation to the 5′-deoxyadenosyl radical.
Purification and structural elucidation of a cobalamin-dependent radical SAM enzyme
- Biology, ChemistryMethods in Enzymology
- 2022
An Unprecedented Ring-Contraction Mechanism in Cobalamin-Dependent Radical S-Adenosylmethionine Enzymes.
- ChemistryThe journal of physical chemistry letters
- 2020
A unique member of the family of cobalamin (Cbl)-dependent radical S-adenosylmethionine (SAM) enzymes, OxsB, catalyzes the ring constriction of deoxyadenosine triphosphate (dATP) to the base oxetane…
Methanogenesis marker protein 10 (Mmp10) from Methanosarcina acetivorans is a radical S-adenosylmethionine methylase that unexpectedly requires cobalamin
- Biology, ChemistryThe Journal of Biological Chemistry
- 2019
The purified and biochemically characterized the radical S-adenosylmethionine (SAM) protein MaMmp10, the product of the methanogenesis marker protein 10 gene in the methane-producing archaea Methanosarcina acetivorans and suggest that cobalamin-dependent radical SAM proteins are more prevalent than previously thought.
Cobalamin-Dependent Radical S-Adenosylmethionine Enzymes: Capitalizing on Old Motifs for New Functions
- BiologyACS bio & med chem Au
- 2022
This work capitalize on the three recent structures of Cbl-dependent radical SAM enzymes that use common cofactors to facilitate ring contraction as well as radical-based and non-radical-based methylation reactions.
References
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- 2013
In vitro activity of GenK, a Cbl-dependent radical SAM enzyme that methylates an unactivated sp(3) carbon during the biosynthesis of gentamicin, an aminoglycoside antibiotic, is demonstrated and one mechanistic possibility for the GenK reaction can be ruled out.
Role of the [4Fe-4S] cluster in reductive activation of the cobalt center of the corrinoid iron-sulfur protein from Clostridium thermoaceticum during acetate biosynthesis.
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The combined results strongly indicate that the FeS cluster of the CFeSP is necessary for reductive activation of Co(II) to Co(I) by physiological reductants but is not required for catalysis, e.g., demethylation of CH3-H4folate or methylation of CODH/ACS.
Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a Mössbauer spectroscopic study.
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- 2002
A dual-iron-isotope (56Fe/57Fe) approach is employed to demonstrate the existence of a unique Fe site in the [4Fe-4S] cluster of PFL-AE by Mössbauer spectroscopy, indicating that AdoMet coordination is a necessary prerequisite to adenosyl radical generation.
Reconstitution and Characterization of the Polynuclear Iron-Sulfur Cluster in Pyruvate Formate-lyase-activating Enzyme
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The iron-sulfur cluster complement proved to be a prerequisite for effective binding of adenosylmethionine, which induces a characteristic shift of the EPR signal shape of the reduced enzyme form ([4Fe-4S]+) from axial to rhombic symmetry.
Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy.
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The electron paramagnetic resonance (EPR) properties of the [Fe-S] clusters are described, which are consistent with the formulation [4Fe-4S] and are adequately simulated by a rhombic spectrum.
Reductive activation of the methyl-tetrahydromethanopterin: coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH
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- 2004
The results support a role for a corrinoid protein in the methyl-tetrahydromethanopterin: HS-CoM methyltransferase reaction at which ATP is involved in the activation of this protein, probably in the conversion of inactive B12a or B12r to active B12s.
Initial characterization of Fom3 from Streptomyces wedmorensis: The methyltransferase in fosfomycin biosynthesis.
- Biology, ChemistryArchives of biochemistry and biophysics
- 2014
Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme.
- ChemistryBiochemistry
- 2007
The energetics of the reductive cleavage of SAM is an outstanding question in the actions of radical SAM enzymes and is here reported for the action of lysine 2,3-aminomutase (LAM), which catalyzes the interconversion of l-lysine and l-beta-lysines.
A Radically Different Mechanism for S-Adenosylmethionine–Dependent Methyltransferases
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The mechanisms of two reactions targeting the sp2-hybridized carbons at positions 2 and 8 of adenosine 2503 in 23S ribosomal RNA, catalyzed by RlmN and Cfr, respectively are determined.
Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions.
- Chemistry, BiologyBiochemistry
- 2001
The results indicate that the dominant stable cluster state for biotin synthase is a dimer containing two [2Fe-2S](2+) and two [4Fe-4S]-2+) clusters.