sodium mercaptopyruvate
sodium mercaptopyruvate structure
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Common Name | sodium mercaptopyruvate | ||
|---|---|---|---|---|
| CAS Number | 10255-67-1 | Molecular Weight | 142.10900 | |
| Density | 1.432g/cm3 | Boiling Point | 227.7ºC at 760mmHg | |
| Molecular Formula | C3H3NaO3S | Melting Point | 200ºC (dec.)(lit.) | |
| MSDS | Chinese USA | Flash Point | 91.5ºC | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase.
J. Biol. Chem. 288(27) , 20002-13, (2013) Mercaptopyruvate sulfurtransferase (MST) is a source of endogenous H2S, a gaseous signaling molecule implicated in a wide range of physiological processes. The contribution of MST versus the other two H2S generators, cystathionine β-synthase and γ-cystathiona... |
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Identification of putative sulfurtransferase genes in the extremophilic Acidithiobacillus ferrooxidans ATCC 23270 genome: structural and functional characterization of the proteins.
OMICS 9(1) , 13-29, (2005) Eight nucleotide sequences containing a single rhodanese domain were found in the Acidithiobacillus ferrooxidans ATCC 23270 genome: p11, p14, p14.3, p15, p16, p16.2, p21, and p28. Amino acids sequence comparisons allowed us to identify the potentially catalyt... |
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Properties of the Escherichia coli rhodanese-like protein SseA: contribution of the active-site residue Ser240 to sulfur donor recognition.
FEBS Lett. 500(3) , 153-6, (2001) The product of Escherichia coli sseA gene (SseA) was the subject of the present investigation aimed to provide a tool for functional classification of the bacterial proteins of the rhodanese family. E. coli SseA contains the motif CGSGVTA around the catalytic... |
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Novel, orally effective cyanide antidotes.
J. Med. Chem. 50(26) , 6462-4, (2007) A series of prodrugs of 3-mercaptopyruvate (3-MP), the substrate for the enzyme 3-mercaptopyruvate/cyanide sulfurtransferase (3-MPST) that converts cyanide to the nontoxic thiocyanate, which are highly effective cyanide antidotes, have been developed. These p... |
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Alternative sulphur donors for detoxification of cyanide in the chicken.
Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. 99(3) , 309-15, (1991) 1. Urinary excretion of thiocyanate by hens after dosage with cyanide was studied over 3 hr periods during which various sulphur sources were infused. 2. With 20 mumoles cyanide, endogenous sulphur supplies appeared to be almost sufficient. 3. With 45 mumoles... |
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Electron paramagnetic resonance evidence for a cysteine-based radical in pyruvate formate-lyase inactivated with mercaptopyruvate.
Biochemistry 34(17) , 5712-7, (1995) Pyruvate formate-lyase (PFL) is a glycyl radical-containing enzyme that catalyzes the reversible, nonoxidative conversion of pyruvate and CoA into acetyl-CoA and formate. The radical is located on the alpha-carbon of glycine 734 and is required for catalysis.... |
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Modifiers of mercaptopyruvate sulfurtransferase catalyzed conversion of cyanide to thiocyanate in vitro.
J. Biochem. Toxicol. 7(2) , 65-72, (1992) The enzyme mercaptopyruvate sulfurtransferase appears to play an important role in the in vivo detoxification of cyanide. It does so by transferring sulfur to cyanide to produce thiocyanate, which is less toxic and may be excreted through the kidney. Several ... |
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3-Mercaptopyruvate, 3-mercaptolactate and mercaptoacetate.
Meth. Enzymol. 143 , 178-82, (1987)
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The combination of cobinamide and sulfanegen is highly effective in mouse models of cyanide poisoning.
Clin. Toxicol. (Phila.) 49(5) , 366-73, (2011) Cyanide is a component of smoke in residential and industrial fires, and accidental exposure to cyanide occurs in a variety of industries. Moreover, cyanide has the potential to be used by terrorists, particularly in a closed space such as an airport or train... |
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Purification and characterization of 3-mercaptopyruvic acid S-conjugate reductases.
Biochem. Pharmacol. 40(9) , 2047-57, (1990) Three kinds of 3-mercaptopyruvic acid S-conjugate reductase (MPR-I, MPR-II and MPR-III) were purified from rat liver cytosol. These enzymes reduced 3-mercaptopyruvic acid S-conjugates derived from cysteine conjugates and some endogenous alpha-keto acids to th... |