Further Studies on S-Substituted Phosphorothioic Acids. Mixed Lithiumsodium Salts of S-(1-Carboxyethyl) Phosphorothioic Acid and S-(2-Carboxyethyl) Phosphorothioic Acid.

Åkerfeldt, Stig; Hasselquist, Hans; Prange, I.; Dam, Henrik; Sjöberg, Berndt; Toft, Jens

doi:10.3891/acta.chem.scand.15-0575

Cited by 11 publications

(6 citation statements)

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“…At pH <2 hydrolysis slows down according to a mechanism discussed by Åkerfeldt. 20 In another study, 22 it was observed that S-phosphorylated cystamine and S-phosphorylated mercaptopropionic acids undergo hydrolysis at a maximal rate at a pH of 3-4, reaching a half-life of about 15 min. at 37 C. Moreover, thiophilic metal ions such as Ag I and Cu II were efficient promoters of phosphothiolester bond hydrolysis.…”

Section: Stabilitymentioning

confidence: 97%

“…[16][17][18][19] In turn, some chemical properties of S-phosphorylated peptides can be inferred from early studies involving several low molecular S-substituted phosphorothioic acids. 20 In general, this class of compounds is very stable at pH >7 up to 12, 21,22 but is prone to phosphothiolester bond hydrolysis with its maximum rate at a pH of 2-4. At pH <2 hydrolysis slows down according to a mechanism discussed by Åkerfeldt.…”

Section: Stabilitymentioning

confidence: 99%

“…at 37 C. Moreover, thiophilic metal ions such as Ag I and Cu II were efficient promoters of phosphothiolester bond hydrolysis. 22 Until now, only two examples of kinetic studies on hydrolysis of S-phosphorylated peptides have been described. In 1988 Pas and Robillard 23 demonstrated that at pH 4 the KIIVApCDAGMGSSAM peptide loses a phosphate group with a maximum rate comparable to the kinetics of phosphoenolthiopyruvate hydrolysis (half-life 30 min.…”

Section: Stabilitymentioning

confidence: 99%

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Puzzling over protein cysteine phosphorylation – assessment of proteomic tools for S-phosphorylation profiling

Buchowiecka

2014

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Cysteine phosphorylation has recently been discovered in both prokaryotic and eukaryotic systems, and is thought to play crucial roles in signaling and regulation of cellular responses. This article explores the topics of chemical stability of this type of structural modification and the resulting issues regarding affinity enrichment of S-phosphopeptides and their mass spectrometry-based detection in the course of general proteomics studies. Together, this work suggests that the current advances in phosphoproteomic methodologies provide adequate tools for investigating protein cysteine phosphorylation and appear to be immediately available for practical implementation. The article provides useful information necessary for designing experiments in the emerging cysteine phosphoproteomics. The examples of methodological proposals for S-linked phosphorylation detection are included herein in order to stimulate development of new approaches by the phosphoproteomic community.

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Section: Stabilitymentioning

confidence: 97%

Section: Stabilitymentioning

confidence: 99%

Section: Stabilitymentioning

confidence: 99%

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Puzzling over protein cysteine phosphorylation – assessment of proteomic tools for S-phosphorylation profiling

Buchowiecka

2014

Analyst

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“…These are summarized in Table I. they found two rate maxima of hydrolysis, at pH [2][3] and at pH [8][9]. The rate of hydrolysis at pH 2-3 was found to be approximately four times as large as that at pH 8-9. In an earlier paper by Akerfeldt,2 cysteamine S-phosphate was reported to have only one rate maximum, at pH 3.…”

mentioning

confidence: 88%

The Influence of Dicyclohexylcarbodiimide Concentration on the Rate of Phospho Diester Bond Formation

Tomlinson¹,

Tener²

1964

J. Org. Chem.

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During the investigation of biologically active boron compounds in this laboratory, compounds such as 2-aminoacetic diphenylborinic anhydride were formed by heating butyl diphenylborinate with glycine.(C,H5)2BOC4H9 + H2NCH2COOH -0 (CeH6)2BO(ÜcH2NH2 + C4H"OHThe low-molecular weight amino acids, such as glycine, react well without a solvent. A solvent, such as toluene, is more convenient with the higher molecular weight, more soluble amino acids. The white solid products appear to be stable and have not undergone change on storage in air for 4 years. These anhydrides may be recrystallized from alcohol-water without change, but they react readily with ethanolamine to form 2-aminoethyl diphenylborinate. ExperimentalAll melting points were obtained on a Fischer-Johns melting point apparatus and were corrected by comparison with standard compounds.Reaction with Glycine.-A mixture of 0.50 g. (0.0067 mole) of glycine and 1.59 g. (0.0067 mole) of butyl diphenylborinate3 was boiled and stirred for 5 min. The mixture became solid.Toluene (5 ml.) was added, and the mixture was boiled for a few minutes. After cooling, the solid was collected on a filter and was washed with ether. The anhydride was boiled with 25 ml. of distilled water and was collected on a filter after cooling, 0.82 g., m.p. 244-245°, 51% (based on butyl diphenylborinate). A 0.33-g. portion was dissolved in 5 ml. of 95% ethanol, filtered while hot, cooled, and recrystallized once more from ethanol to yield 0.13 g., m.p. 244-245°.

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“…Protonation was carried out by adding varying amounts of D2G (1,2,4,6,8, and 10 equiv) followed by rapid stirring for 5 ± 0.5 min. The appearance of the protonation mixture varied.…”

mentioning

confidence: 99%

Protonation of the indole Grignard reagent and other organometallic derivatives of indole

Powers¹,

Meyer²,

Parsons³

1967

J. Am. Chem. Soc.

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Further Studies on S-Substituted Phosphorothioic Acids. Mixed Lithiumsodium Salts of S-(1-Carboxyethyl) Phosphorothioic Acid and S-(2-Carboxyethyl) Phosphorothioic Acid.

Cited by 11 publications

References 0 publications

Puzzling over protein cysteine phosphorylation – assessment of proteomic tools for S-phosphorylation profiling

Puzzling over protein cysteine phosphorylation – assessment of proteomic tools for S-phosphorylation profiling

The Influence of Dicyclohexylcarbodiimide Concentration on the Rate of Phospho Diester Bond Formation

Protonation of the indole Grignard reagent and other organometallic derivatives of indole

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