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目录号 : GC48066

A radical SAM enzyme substrate

SAHO2 Chemical Structure

Cas No.:53199-56-7

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1 mg
¥770.00
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5 mg
¥3,667.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

SAHO2 is a sulfone form of the methyl donor S-(5'-adenosyl)-L-methionine chloride and is a substrate for radical SAM enzymes.1 It is reductively cleaved to 5'-deoxyadenosine and 5'-thioadenosine sulfinic acid by the radical SAM enzymes NosL or NosN.

1.Mandalapu, D., Ji, X., and Zhang, Q.Reductive cleavage of sulfoxide and sulfone by two radical S-adenosyl-L-methionine enzymesBiochemistry58(1)36-39(2019)

Chemical Properties

Cas No. 53199-56-7 SDF
Canonical SMILES O[C@H]1[C@@H](O)[C@@](N2C=NC3=C(N)N=CN=C32)([H])O[C@@H]1CS(CC[C@H](N)C(O)=O)(=O)=O
分子式 C14H20N6O7S 分子量 416.4
溶解度 DMSO: 30 mg/ml,PBS (pH 7.2): 10 mg/ml 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 2.4015 mL 12.0077 mL 24.0154 mL
5 mM 0.4803 mL 2.4015 mL 4.8031 mL
10 mM 0.2402 mL 1.2008 mL 2.4015 mL
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Research Update

Reductive Cleavage of Sulfoxide and Sulfone by Two Radical S-Adenosyl-l-methionine Enzymes

Biochemistry 2019 Jan 8;58(1):36-39.PMID:30398855DOI:10.1021/acs.biochem.8b00844.

Sulfoxides and sulfones are commonly found in nature as a result of thioether oxidation, whereas only a very few enzymes have been found to metabolize these compounds. Utilizing the strong reduction potential of the [4Fe-4S] cluster of radical S-adenosyl-l-methionine (SAM) enzymes, we herein report the first enzyme-catalyzed reductive cleavage of sulfoxide and sulfone. We show two radical SAM enzymes, tryptophan lyase NosL and the class C radical SAM methyltransferase NosN, are able to act on a sulfoxide SAHO and a sulfone SAHO2, both of which are structurally similar to SAM. NosL cleaves all of the three bonds (i.e., S-C(5'), S-C(γ), and S-O) connecting the sulfur center of SAHO, with a preference for S-C(5') bond cleavage. Similar S-C cleavage activity was also found for SHAO2, but no S-O cleavage was observed. In contrast to NosL, NosN almost exclusively cleaves the S-C(5') bonds of SAHO and SAHO2 with much higher efficiencies. Our study provides valuable insights into the [4Fe-4S] cluster-mediated reduction reactions and highlights the remarkable catalytic promiscuity of radical SAM enzymes.