2464-23-5

Usage

Uses

Used in Pharmaceutical Industry:
Propanoic acid, 3-mercapto-2-oxo-, is used as an intermediate in the synthesis of various pharmaceutical compounds. Its unique structure allows it to be a key component in the development of drugs targeting specific biological pathways.
Used in Chemical Synthesis:
In the chemical industry, Propanoic acid, 3-mercapto-2-oxo-, is utilized as a building block for the synthesis of complex organic molecules. Its distinct functional groups enable it to participate in various chemical reactions, leading to the formation of a wide range of products.
Used in Research and Development:
Due to its unique structure and properties, Propanoic acid, 3-mercapto-2-oxo-, is employed in research and development for studying the effects of structural modifications on the biological activity of compounds. It can be used to investigate the role of specific functional groups in molecular interactions and their impact on biological systems.
Used in Analytical Chemistry:
Propanoic acid, 3-mercapto-2-oxo-, can be used as a reference compound or a standard in analytical chemistry for the calibration of instruments and the development of new analytical methods. Its distinct properties make it suitable for various applications in this field.

Upstream product

• 921-01-7 D-cysteine 
• 52-90-4 L-Cysteine 
• 1113-59-3 bromopyruvic acid 
• 507-09-5 tiolacetic acid 
• 52-89-1 l-cysteine hydrochloride 
• 328-50-7 α-ketoglutaric acid 

Downstream Products

• 117373-19-0 2-(2,4-dinitro-phenylhydrazono)-3-mercapto-propionic acid 
• 2614-83-7 3-mercaptolactate 

Relevant academic research and scientific papers

Deciphering Nature's Intricate Way of N,S-Dimethylating l -Cysteine: Sequential Action of Two Bifunctional Adenylation Domains

Dimethylation of amino acids consists of an interesting and puzzling series of events that could be achieved, during nonribosomal peptide biosynthesis, either by a single adenylation (A) domain interrupted by a methyltransferase (M) domain or by the sequential action of two of such independent enzymes. Herein, to establish the method by which Nature N,S-dimethylates l-Cys, we studied its formation during thiochondrilline A biosynthesis by evaluating TioS(A3aM3SA3bT3) and TioN(AaMNAb). This study not only led to identification of the exact pathway followed in Nature by these two enzymes for N,S-dimethylation of l-Cys, but also revealed that a single interrupted A domain can N,N-dimethylate amino acids, a novel phenomenon in the nonribosomal peptide field. These findings offer important and useful insights for the development and engineering of novel interrupted A domain enzymes to serve, in the future, as tools for combinatorial biosynthesis.

Condensation of Macrocyclic Polyketides Produced by Penicillium sp. DRF2 with Mercaptopyruvate Represents a New Fungal Detoxification Pathway

Application of a refined procedure of experimental design and chemometric analysis to improve the production of curvularin-related polyketides by a marine-derived Penicillium sp. DRF2 resulted in the isolation and identification of cyclothiocurvularins 6-8 and cyclosulfoxicurvularins 10 and 11, novel curvularins condensed with a mercaptolactate residue. Two additional new curvularins, 3 and 4, are also reported. The structures of the sulfur-bearing curvularins were unambiguously established by analysis of spectroscopic data and by X-ray diffraction analysis. Analysis of stable isotope feeding experiments with [U-13C315N]-l-cysteine confirmed the presence of the 2-hydroxy-3-mercaptopropanoic acid residue in 6-8 and the oxidized sulfoxide in 10 and 11. Cyclothiocurvularins A (6) and B (7) are formed by spontaneous reaction between 10,11-dehydrocurvularin (2) and mercaptopyruvate (12) obtained by transamination of cysteine. High ratios of [U-13C315N]-l-cysteine incorporation into cyclothiocurvularin B (7), the isolation of two diastereomers of cyclothiocurvularins, the lack of cytotoxicity of cyclothiocurvularin B (7) and its methyl ester (8), and the spontaneous formation of cyclothiocurvularins from 10,11-dehydrocurvularin and mercaptopyruvate provide evidence that the formation of cyclothiocurvularins may well correspond to a 10,11-dehydrocurvularin detoxification process by Penicillium sp. DRF2.

In vitro biosynthesis of 3-mercaptolactate by lactate dehydrogenases

3-Mercaptolactate (3ML) is an interesting mercapto compound with special regard to the biosynthesis of new polythioesters (PTEs). Unfortunately, this thioester analog of lactic acid is currently not commercially available. For this reason, we developed an in vitro biosynthesis pathway to convert cysteine to 3-mercaptopyruvate (3MPy), which is then rapidly and efficiently converted to 3ML by suitable lactate dehydrogenases (LDHs). As liver LDH from Rattus norvegicus (LDHRn) was previously described to Exhibit 3MPy reduction activity, in silico studies based on homology to LDHRn were performed and led to the identification of four potentially suitable bacterial LDH candidates from Escherichia coli (LDHEc), Corynebacterium glutamicum (LDHCg), Bacillus cereus (LDHBc) and Gloeobacter violaceus (LDHGv). After heterologous expression in E. coli followed by purification, the enzymes were assessed for their potential to reduce 3MPy to 3ML in comparison to LDHRn. With 3MPy, LDHs from E. coli, C. glutamicum and B. cereus showed no or only very low specific activities of 0.23 ± 0.1 U/mg (LDHCg) and 0.08 ± 0.2 U/mg (LDHBc), respectively. In contrast, LDHGv exhibited a remarkable specific activity of 63.6 ± 8.1 U/mg, being even twice as active as the R. norvegicus LDH. To verify LDH-catalyzed biosynthesis of 3ML we developed and optimized a detection method allowing qualitative analysis and quantification of 3MPy and 3ML by derivatization with Ellman's reagent and liquid chromatography-mass spectrometry. This study shows once more the impressive versatility of LDHs and presents a rapid and efficient biosynthesis process for 3ML, a biotechnologically interesting, yet hard-to-obtain, compound.

Synthesis, Characterisation and Reactivity of 3-Mercaptopyruvic Acid

The synthesis, isolation and spectroscopic characterisation of the sulfur metabolic compound 3-mercaptopyruvic acid (3-MPH) is reported, for the first time. The compound is isolated without tedious workup, with a purity of 97 %, as indicated by chemical and biochemical analyses. Detailed kinetic and thermodynamic studies of its complex behaviour in solution are discussed. 3-MPH is stable in the enol form in non-polar solvent. In polar solvent, a fast equilibrium between the α-ketoacid and a cyclic dimer dithiane is observed. The formation of the dimer confers increased stability to 3-MPH towards hydrogen peroxide, in comparison with cysteine.

The pseudoalteromonas luteoviolacea L-amino acid oxidase with antimicrobial activity is a flavoenzyme

The marine environment is a rich source of antimicrobial compounds with promising pharmaceutical and biotechnological applications. The Pseudoalteromonas genus harbors one of the highest proportions of bacterial species producing antimicrobial molecules. For decades, the presence of proteins with L-amino acid oxidase (LAAO) and antimicrobial activity in Pseudoalteromonas luteoviolacea has been known. Here, we present for the first time the identification, cloning, characterization and phylogenetic analysis of Pl-LAAO, the enzyme responsible for both LAAO and antimicrobial activity in P. luteoviolacea strain CPMOR-2. Pl-LAAO is a flavoprotein of a broad substrate range, in which the hydrogen peroxide generated in the LAAO reaction is responsible for the antimicrobial activity. So far, no protein with a sequence similarity to Pl-LAAO has been cloned or characterized, with this being the first report on a flavin adenine dinucleotide (FAD)-containing LAAO with antimicrobial activity from a marine microorganism. Our results revealed that 20.4% of the sequenced Pseudoalteromonas strains (specifically, 66.6% of P. luteoviolacea strains) contain Pl-laao similar genes, which constitutes a well-defined phylogenetic group. In summary, this work provides insights into the biological significance of antimicrobial LAAOs in the Pseudoalteromonas genus and shows an effective approach for the detection of novel LAAOs, whose study may be useful for biotechnological applications.

Isolation, purification, and characterization of phenylpyruvate transaminating enzymes of Erwinia carotovora

Enzymes of Erwinia carotovora that transaminate phenylpyruvate were isolated, purified, and characterized. Two aromatic aminotransferases (PAT1 and PAT2) and an aspartic aminotransferase (PAT3) were found. According to gel filtration, these enzymes have molecular weights of 76, 75, and 78 kDa. The enzymes consist of two identical subunits of molecular weights of 31.4, 31, and 36.5 kDa, respectively. The isoelectric points of PAT1, PAT2, and PAT3 were determined as 3.6, 3.9, and 4.7, respectively. The enzyme preparations considerably differ in substrate specificity. All three of the enzymes productively interacted with the following amino acids: L-aspartic acid, L-leucine (except PAT3), L-isoleucine (except PAT3), L-serine, L-methionine, L-cysteine, L-phenylalanine, L-tyrosine, and L-tryptophane. The aromatic aminotransferases display higher specificity to the aromatic amino acids and the leucine-isoleucine pair, whereas the aspartic aminotransferase displays higher specificity to L-aspartic acid and relatively low specificity to the aromatic amino acids. The aspartic aminotransferase does not use L-leucine or L-isoleucine as a substrate. PAT1, PAT2, and PAT3 show the highest activity at pH 8.9 and at 48, 53, and 58°C, respectively.

Role of the active site residues arginine-216 and arginine-237 in the substrate specificity of mammalian D-aspartate oxidase

d-Aspartate oxidase (DDO) and d-amino acid oxidase (DAO) are flavin adenine dinucleotide-containing flavoproteins that catalyze the oxidative deamination of d-amino acids. Unlike DAO, which acts on several neutral and basic d-amino acids, DDO is highly specific for acidic d-amino acids. Based on molecular modeling and simulated annealing docking analyses, a recombinant mouse DDO carrying two substitutions (Arg-216 to Leu and Arg-237 to Tyr) was generated (R216L-R237Y variant). This variant and two previously constructed single-point mutants of mouse DDO (R216L and R237Y variants) were characterized to investigate the role of Arg-216 and Arg-237 in the substrate specificity of mouse DDO. The R216L-R237Y and R216L variants acquired a broad specificity for several neutral and basic d-amino acids, and showed a considerable decrease in activity against acidic d-amino acids. The R237Y variant, however, did not show any additional specificity for neutral or basic d-amino acids and its activity against acidic d-amino acids was greatly reduced. The kinetic properties of these variants indicated that the Arg-216 residue is important for the catalytic activity and substrate specificity of mouse DDO. However, Arg-237 is, apparently, only marginally involved in substrate recognition, but is important for catalytic activity. Notably, the substrate specificity of the R216L-R237Y variant differed significantly from that of the R216L variant, suggesting that Arg-237 has subsidiary effects on substrate specificity. Additional experiments using several DDO and DAO inhibitors also suggested the involvement of Arg-216 in the substrate specificity and catalytic activity of mouse DDO and that Arg-237 is possibly involved in substrate recognition by this enzyme. Collectively, these results indicate that Arg-216 and Arg-237 play crucial and subsidiary role(s), respectively, in the substrate specificity of mouse DDO.