Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

AG-K-50018 (2S)-2-amino-3- hydroxysulfanyl-propanoic acid

Synonyms: CHEBI:41710, Cys(OH), AC1L4WIO, AC1Q5QNT, AR-1L4175, ...

Claiborne, A. et al., Argyrou, A. et al., Luba, J. et al., Claiborne, A. et al., Dierks, T. et al., et al.

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Disease relevance of Cys-sulfenic acid

Furthermore, the CoADR sequence reveals the presence of a single putative active-site Cys (Cys43) within an SFXXC motif also seen in the Enterococcus faecalis NADH oxidase and NADH peroxidase, which use a single redox-active cysteine-sulfenic acid in catalysis [1].

High impact information on Cys-sulfenic acid

The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate [2].
However, chemical and spectroscopic evidence demonstrate that the non-flavin redox center in NADH peroxidase is an unusual stabilized cysteine-sulfenic acid (Cys-SOH) derivative, and not a cystine disulfide as found in the disulfide reductases [3].
The active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in the crystal, is located at the bottom of a relatively narrow pocket [4].
The nature of the nonflavin redox center located adjacent to the flavin varies and three types have been identified: an enzymic disulfide (most commonly), an enzymic cysteine sulfenic acid (NADH peroxidase and NADH oxidase), and a mixed Cys-S-S-CoA disulfide (coenzyme A disulfide reductase) [5].
In contrast, oxidations of cysteinyl side chains in proteins, where disulfide bond formation can be prevented and where the reactivity of the nascent cysteine-sulfenic acid (Cys-SOH) can be controlled, have previously been shown to yield stable active-site Cys-SOH derivatives of papain and glyceraldehyde-3-phosphate dehydrogenase [6].

Associations of Cys-sulfenic acid with other chemical compounds

Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite [7].

Gene context of Cys-sulfenic acid

Peroxide modification of monoalkylated glutathione reductase. Stabilization of an active-site cysteine-sulfenic acid [8].
BCP exists as a monomer, and its functional Cys-45 appeared to exist as cysteine sulfenic acid [9].

Analytical, diagnostic and therapeutic context of Cys-sulfenic acid

Reductive titrations and thiol analyses confirm the presence of the unusual cysteine-sulfenic acid (Cys-SOH) redox center identified previously [10].

References

Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides. Luba, J., Charrier, V., Claiborne, A. Biochemistry (1999) [Pubmed]
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., von Figura, K., Ficner, R., Rudolph, M.G. Cell (2005) [Pubmed]
Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response. Claiborne, A., Ross, R.P., Parsonage, D. Trends Biochem. Sci. (1992) [Pubmed]
Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Choi, H.J., Kang, S.W., Yang, C.H., Rhee, S.G., Ryu, S.E. Nat. Struct. Biol. (1998) [Pubmed]
Flavoprotein disulfide reductases: advances in chemistry and function. Argyrou, A., Blanchard, J.S. Prog. Nucleic Acid Res. Mol. Biol. (2004) [Pubmed]
Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. Claiborne, A., Miller, H., Parsonage, D., Ross, R.P. FASEB J. (1993) [Pubmed]
Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite. Peshenko, I.V., Shichi, H. Free Radic. Biol. Med. (2001) [Pubmed]
Peroxide modification of monoalkylated glutathione reductase. Stabilization of an active-site cysteine-sulfenic acid. Miller, H., Claiborne, A. J. Biol. Chem. (1991) [Pubmed]
Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family. Jeong, W., Cha, M.K., Kim, I.H. J. Biol. Chem. (2000) [Pubmed]
Purification and analysis of streptococcal NADH peroxidase expressed in Escherichia coli. Parsonage, D., Miller, H., Ross, R.P., Claiborne, A. J. Biol. Chem. (1993) [Pubmed]

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