33239-40-6

Basic information

• Product Name: 2-oxosuccinamic acid
• Synonyms: 2-oxosuccinamic acid;4-Amino-2,4-dioxobutanoic acid;alpha-Ketosuccinamic acid
• CAS NO: 33239-40-6
• Molecular Formula: C₄H₅NO₄
• Molecular Weight: 131.09
• Mol File: 33239-40-6.mol
• Article Data: 6

Chemical Properties

• Melting Point: 140℃
• Boiling Point: 374.9°Cat760mmHg
• Flash Point: 180.5°C
• Appearance: /
• Density: 1.504g/cm³
• Vapor Pressure: 1.18E-06mmHg at 25°C
• Refractive Index: 1.502
• PKA: 2.38±0.54(Predicted)
• CAS DataBase Reference: 2-oxosuccinamic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 2-oxosuccinamic acid(33239-40-6)
• EPA Substance Registry System: 2-oxosuccinamic acid(33239-40-6)

Safety Data

• Hazardous Substances Data: 33239-40-6(Hazardous Substances Data)

Usage

InChI:InChI=1/C4H5NO4/c5-3(7)1-2(6)4(8)9/h1H2,(H2,5,7)(H,8,9)

Upstream product

• 70-47-3 L-asparagine 
• 54468-53-0 4-amino-2-methylene-4-oxo-butanoic acid 
• 95-92-1 oxalic acid diethyl ester 
• 2058-58-4 (R)-Asparagine 

Relevant articles and documents

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.

PREPARATION OF 4-AMINO-2,4-DIOXOBUTANOIC ACID

A process for synthesizing 4-amino-2,4-dioxobutanoic acid involves reacting diethyl oxalate with sodium ethoxide in ethanol to form a reaction mixture, and afterward adding 2-cyano-3-hydroxy-butenedioate to the reaction mixture and allowing a reaction to proceed under conditions suitable to form a first reaction product of the formula diethyl-2-cyano-3-hydroxy-butenedioate, and then isolating the cyano-3-hydroxy-butenedioate, and afterward reacting the diethyl-2-cyano-3-hydroxy-butenedioate with aqueous sodium hydroxide under conditions suitable to form 4-amino-2,4-dioxobutanoic acid.

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.