The structure of dehydromethionine. An azasulfonium salt

Glass, Richard S.; Duchek, John R.

doi:10.1021/ja00420a016

Cited by 31 publications

(16 citation statements)

References 6 publications

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“…[8,40] This molecule can be prepared via photo-oxidation or via oxidation by iodine. The molecule is stable under physiological pH, it decomposes in the excess of iodide or in acidic solution.…”

Section: Structure Of the Met-lys Cross-linking Bondmentioning

confidence: 99%

Novel Covalent Bond in Proteins: Calculations on Model Systems Question the Bond Stability

Ončák¹,

Berka²,

Slavı́ček³

2011

ChemPhysChem

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We have investigated the sulfilimine covalent link between methionine (Met) and lysine (Lys), recently identified in collagen IV (R. Vanacore, A.-J. L. Ham, M. Voehler, C. R. Sanders, T. P. Conrads, T. D. Veenstra, K. B. Sharpless, P. E. Dawson, B. G. Hudson, Science 2009, 325, 1230), and have explored its stability with respect to both the redox processes and UV radiation by means of advanced computational methods. We have concluded that the bond should be present in a protonated state, (-NH=S-)(+). The bond is characterized by a relatively high standard reduction potential, that is, the bond should not be stable in a typical cell environment; if the sulfilimine bond exists (as suggested by the experiment) then the bond has to be supported by the protein environment. The sulfilimine bond then destabilizes the protein structure with respect to the alternative tertiary structure. We discuss conditions under which the bond could be formed as well as other possible structural arrangements consistent with the Met-Lys stoichiometry; some of the alternative bond motifs are more thermodynamically stable than the sulfilimine bond. We suggest that the character of the Met-Lys contact could be approached via NEXAFS spectroscopy. Finally, we show that the protonation brings photostability to the sulfilimine bond.

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Section: Structure Of the Met-lys Cross-linking Bondmentioning

confidence: 99%

Novel Covalent Bond in Proteins: Calculations on Model Systems Question the Bond Stability

Ončák¹,

Berka²,

Slavı́ček³

2011

ChemPhysChem

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“…Most sulfilimines that have been reported are stabilized by strong electron withdrawing groups on the nitrogen end of the sulfilimine linkage (23). However, cyclic sulfilimines derived from the oxidation of methionine analogs by I 2 have been characterized in detail as their isothiazolidinium salts following protonation of the nitrogen (24, 25). These studies showed direct bonding of the nitrogen and sulfur atoms and a new stereogenic center at the sulfur atom, consistent with the two methyl resonances seen by NMR.…”

mentioning

confidence: 99%

A Sulfilimine Bond Identified in Collagen IV

Vanacore

Ham

Voehler

et al. 2009

Science

225

196

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Collagen IV networks are ancient proteins of basement membranes that underlie epithelia in metazoa from sponge to human. The networks provide structural integrity to tissues and serve as ligands for integrin cell-surface receptors. They are assembled by oligomerization of triple-helical protomers and are covalently cross-linked, a key reinforcement that stabilizes networks. We used Fourier-transform ion cyclotron resonance mass spectrometry and nuclear magnetic resonance spectroscopy to show that a sulfilimine bond (-S=N-) crosslinks hydroxylysine-211 and methionine-93 of adjoining protomers, a bond not previously found in biomolecules. This bond, the nitrogen analog of a sulfoxide, appears to have arisen at the divergence of sponge and cnidaria, an adaptation of the extracellular matrix in response to mechanical stress in metazoan evolution.

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“…The sulfilimine bond is known to exist in nature in the form of dehydromethionine 8. 40 This molecule can be prepared via photo‐oxidation or via oxidation by iodine. The molecule is stable under physiological pH, it decomposes in the excess of iodide or in acidic solution.…”

Section: Resultsmentioning

confidence: 99%

Systematic Synthesis of Bisubstrate‐Type Inhibitors of N‐Acetylglucosaminyltransferases

Hanashima

Inamori

Manabe

et al. 2006

Chemistry A European J

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Bisubstrate-type inhibitors for N-acetylglucosaminyltransferase (GnT)-V and -IX were designed and synthesized. These compounds carry both an acceptor trisaccaride and an UDP-GlcNAc component tethered by a linker of variable length. The acceptor trisaccharide unit was constructed using a combination of a polymer support and a resin capture-release strategy. Namely, starting with a beta-mannoside bound to low molecular weight monomethyl PEG (MPEG), successive glycosylations with donors having chloroacetyl group produced the trisaccharide, which was subjected to the capture-release purification using cysteine loaded resin. UDP-GlcNAc units carrying phosphate moieties were separately synthesized from the bromoacetamide-containing glucosamine derivative. Ligation between the acceptor thiol and each alkyl bromide on the donor unit readily proceeded, and produced the coupling product. The introduction of the UMP component gave target compounds. All of the synthesized compounds had significant activities to GnT-V and -IX. Their potencies were dependent upon the linkers length. GnT-IX was more sensitive to these inhibitors and optimum linker length was clearly different between these GnTs. The most potent inhibitor of GnT-V had Ki=18.3 microM, while that of GnT-IX had Ki = 4.7 microM.

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The structure of dehydromethionine. An azasulfonium salt

Cited by 31 publications

References 6 publications

Novel Covalent Bond in Proteins: Calculations on Model Systems Question the Bond Stability

Novel Covalent Bond in Proteins: Calculations on Model Systems Question the Bond Stability

A Sulfilimine Bond Identified in Collagen IV

Systematic Synthesis of Bisubstrate‐Type Inhibitors of N‐Acetylglucosaminyltransferases

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