38335-24-9

Usage

Uses

Used in Pharmaceutical Research:
P-Nitrophenylpyruvic acid is used as a key intermediate in the synthesis of various pharmaceutical agents. Its unique structure and reactivity make it a valuable component in the development of new therapeutic compounds.
Used in Biochemical Research:
P-Nitrophenylpyruvic acid is used as a substrate for the enzyme alanine transaminase, which plays a crucial role in the metabolism of amino acids. It aids in studying enzyme kinetics and understanding the mechanisms of amino acid metabolism.
Used in Enzyme Assays:
P-Nitrophenylpyruvic acid is employed in enzyme assays to measure the activity of alanine transaminase. The release of the nitrophenyl group upon enzymatic reaction allows for the quantification of enzyme activity, providing insights into metabolic processes and potential therapeutic targets.
Used in Drug Development:
P-Nitrophenylpyruvic acid is utilized in the development of new drugs targeting alanine transaminase and related metabolic pathways. Its unique properties enable the design of compounds with enhanced efficacy and selectivity, contributing to the advancement of pharmaceutical therapies.

InChI:InChI=1/C9H7NO5/c11-8(9(12)13)5-6-1-3-7(4-2-6)10(14)15/h1-4H,5H2,(H,12,13)

Upstream product

• 99-99-0 1-methyl-4-nitrobenzene 
• 95-92-1 oxalic acid diethyl ester 
• 860189-96-4 3-cyano-3-(4-nitro-phenyl)-2-oxo-propionic acid ethyl ester 
• 79547-05-0 ethyl (4-nitrophenyl)pyruvate 
• 16921-36-1 3-(4-aminophenyl)-2-oxopropanoic acid 
• 1991-83-9 4-nitrophenylalanine 
• 619-89-6 p-nitrocinnamic acid 
• 949-99-5 4-nitro-3-phenyl-L-alanine 
• 70973-01-2 2-acetamido-3-(4-nitrophenyl)acrylic acid 
• 555-16-8 4-nitrobenzaldehdye 
• 711015-30-4 2-methyl-4-[(E)-(4-nitrophenyl)methylidene]-1,3-oxazol-5(4H)-one 
• 1081844-77-0 (2E)-2-(acetylamino)-3-(4-nitrophenyl)prop-2-enoic acid 
• 461-72-3 2,4-imidazolidinedione 

Downstream Products

• 22900-97-6 3-(4-nitro-phenyl)-2-(4-oxo-2-thioxo-thiazolidin-5-ylidene)-propionic acid 
• 117499-14-6 N-(2-aminoethyl)-3-(4-nitrophenyl)alanine dihydrochloride 
• 949-99-5 4-nitro-3-phenyl-L-alanine 
• 92121-68-1 (+)-Obafluorin 
• 99268-39-0 (2S,3R)-2-<(2,3-Dihydroxybenzoyl)amino>-3-hydroxy-4-(4-nitrophenyl)butanoic acid 
• 99268-38-9 (2S,3R)-2-amino-3-hydroxy-4-(4-nitrophenyl)butanoic acid 
• 1460-05-5 p-nitrophenylacetaldehyde 
• 56613-61-7 (R)-4-nitro-phenylalanine 
• 13942-65-9 3-(4-nitrophenyl)-2-oxopropanamide 
• 1567951-64-7 4-(4-methoxyphenyl)-3-(4-nitrophenyl)pyrrole-2-carboxylic acid 
• 117499-10-2 N-(carboxymethyl)-N-(2-(bis(carboxymethyl)amino)ethyl)-3-(4-aminophenyl)alanine 
• 117499-12-4 N-(carboxymethyl)-N-(2-(bis(carboxymethyl)amino)ethyl)-3-(4-isothiocyanatophenyl)alanine dihydrochloride 
• 117499-15-7 N-(carboxymethyl)-N-(2-(bis(carboxymethyl)amino)ethyl)-3-(4-nitrophenyl)alanine 
• 555-16-8 4-nitrobenzaldehdye 

Relevant academic research and scientific papers

β-Lactone formation during product release from a nonribosomal peptide synthetase

Nonribosomal peptide synthetases (NRPSs) are multidomain modular biosynthetic assembly lines that polymerize amino acids into a myriad of biologically active nonribosomal peptides (NRPs). NRPS thioesterase (TE) domains employ diverse release strategies for off-loading thioester-tethered polymeric peptides from termination modules typically via hydrolysis, aminolysis, or cyclization to provide mature antibiotics as carboxylic acids/esters, amides, and lactams/lactones, respectively. Here we report the enzyme-catalyzed formation of a highly strained β-lactone ring during TE-mediated cyclization of a β-hydroxythioester to release the antibiotic obafluorin (Obi) from an NRPS assembly line. The Obi NRPS (ObiF) contains a type I TE domain with a rare catalytic cysteine residue that plays a direct role in β-lactone ring formation. We present a detailed genetic and biochemical characterization of the entire Obi biosynthetic gene cluster in plant-associated Pseudomonas fluorescens ATCC 39502 that establishes a general strategy for β-lactone biogenesis.

Deracemization and Stereoinversion of α-Amino Acids by l-Amino Acid Deaminase

Enantiomerically pure α-amino acids are compounds of primary interest for the fine chemical, pharmaceutical, and agrochemical sectors. Amino acid oxidases are used for resolving d,l-amino acids in biocatalysis. We recently demonstrated that l-amino acid deaminase from Proteus myxofaciens (PmaLAAD) shows peculiar features for biotechnological applications, such as a high production level as soluble protein in Escherichia coli and a stable binding with the flavin cofactor. Since l-amino acid deaminases are membrane-bound enzymes, previous applications were mainly based on the use of cell-based methods. Now, taking advantage of the broad substrate specificity of PmaLAAD, a number of natural and synthetic l-amino acids were fully converted by the purified enzyme into the corresponding α-keto acids: the fastest conversion was obtained for 4-nitrophenylalanine. Analogously, starting from racemic solutions, the full resolution (ee >99%) was also achieved. Notably, d,l-1-naphthylalanine was resolved either into the d- or the l-enantiomer by using PmaLAAD or the d-amino acid oxidase variant having a glycine at position 213, respectively, and was fully deracemized when the two enzymes were used jointly. Moreover, the complete stereoinversion of l-4-nitrophenylalanine was achieved using PmaLAAD and a small molar excess of borane tert-butylamine complex. Taken together, recombinant PmaLAAD represents an l-specific amino acid deaminase suitable for producing the pure enantiomers of several natural and synthetic amino acids or the corresponding keto acids, compounds of biotechnological or pharmaceutical relevance. (Figure presented.).

Bio-inspired enantioselective full transamination using readily available cyclodextrin

The mimics of vitamin B6-dependent enzymes that catalyzed an enantioselective full transamination in the pure aqueous phase have been realized for the first time through the establishment of a new “pyridoxal 5′-phosphate (PLP) catalyzed non-covalent cyclodextrin (CD)-keto acid inclusion complexes” system, and various optically active amino acids have been obtained.

Synthesis of D- and L-Phenylalanine Derivatives by Phenylalanine Ammonia Lyases: A Multienzymatic Cascade Process

The synthesis of substituted D-phenylalanines in high yield and excellent optical purity, starting from inexpensive cinnamic acids, has been achieved with a novel one-pot approach by coupling phenylalanine ammonia lyase (PAL) amination with a chemoenzymatic deracemization (based on stereoselective oxidation and nonselective reduction). A simple high-throughput solid-phase screening method has also been developed to identify PALs with higher rates of formation of non-natural D-phenylalanines. The best variants were exploited in the chemoenzymatic cascade, thus increasing the yield and ee value of the D-configured product. Furthermore, the system was extended to the preparation of those L-phenylalanines which are obtained with a low ee value using PAL amination.

Reactions of Trialkylsilyl Trifluoromethanesulfonates XI. - Synthesis of α-Oxocarboxylic Acid Derivatives from 2-O-Functionalized Trimethylsilyl Ketene Acetals

The cyclic ketene acetals 3, 5 are prepared from the dioxolanone 2 resp. the oxazolidinediones 4 by silylation with trimethylsilyl triflate (1)/triethylamine.In an aldol addition/Peterson olefination reaction catalysed by 1 the ketene acetals 3, 5 yield the (E/Z)-benzylidene derivatives 7, 12, 13 in reaction with aromatic aldehydes 6.In a side reaction the α-(trimethylsilyl)benzylidene derivatives 8 are formed from 3 and 6.Compounds 7 can be hydrolysed to yield α-ketocarboxylic acids 14.The latter are also obtained via β-elimination of trimethylsilanol from 2,3-bis(trimethylsiloxy)carboxylic acid anhydride/DMAP/pyridine. Key Words: 1,3-Dioxolanes / 1,3-Oxazolidines / α-Oxocarboxylic acids

Bifunctional chelating agents

The present invention provides bifunctional chelating agents comprising a unique substrate reactive moiety incorporated into a carboxymethyl arm of a polyaminopolycarboxylate chelating framework capable of forming stable complexes with metal ions.

Synthesis of novel bifunctional chelators and their use in preparing monoclonal antibody conjugates for tumor targeting

Bifunctional derivatives of the chelating agents ethylenediaminetetraacetic acid and diethylenetriaminepentaacetic acid, in which a p-isothiocyanatobenzyl moiety is attached at the methylene carbon atom of one carboxymethyl arm, was synthesized by reducti