18875-37-1

Basic information

• Product Name: L-ALANINE-UL-14C
• Synonyms: ALANINE, L-[14C(U)];L-ALANINE, [1-14C(U)];L-ALANINE, [14C(U)]-;L-ALANINE, [U-14C];L-ALANINE-UL-14C;L-[U-14C]ALANINE;L-alanine-ul-14C mol. wt. 89.1;L-Alanine-UL-14C hydrochloride
• CAS NO: 18875-37-1
• Molecular Formula: C3H7NO2
• Molecular Weight: 95.15
• Mol File: 18875-37-1.mol
• Article Data: 660

Chemical Properties

• Boiling Point: 212.907 °C at 760 mmHg
• Flash Point: 82.563 °C
• Appearance: /aqueous ethanol solution
• Density: 1.161 g/cm³
• Storage Temp.: 2-8°C
• CAS DataBase Reference: L-ALANINE-UL-14C(CAS DataBase Reference)
• NIST Chemistry Reference: L-ALANINE-UL-14C(18875-37-1)
• EPA Substance Registry System: L-ALANINE-UL-14C(18875-37-1)

Safety Data

• Hazard Codes: Xi,R
• Statements: 36/37/38
• Safety Statements: 26-36/37
• RIDADR: UN 2910 7
• WGK Germany: 3
• Hazardous Substances Data: 18875-37-1(Hazardous Substances Data)

Usage

General Description

L-ALANINE-UL-14C is a radioactive form of the amino acid L-alanine that contains a carbon-14 isotope. It is commonly used in biochemical and metabolic studies to track the fate and metabolism of L-alanine in biological systems. The carbon-14 isotope allows for the detection and quantification of L-alanine in various biological samples, making it a valuable tool for research in areas such as protein synthesis, energy metabolism, and amino acid metabolism. L-ALANINE-UL-14C is a crucial chemical in understanding the biochemical processes associated with L-alanine and its role in various physiological and pathological conditions.

InChI:InChI=1/C3H7NO2/c1-2(4)3(5)6/h2H,4H2,1H3,(H,5,6)/t2-/m0/s1

Upstream product

• 6168-72-5 2-Amino-1-propanol 
• 70187-79-0 ethyl 2-N-acetylamino-2-cyanopropionate 
• 55166-91-1 diethyl α-acetamido, α-methylmalonate 
• 109043-92-7 N-(1-[2]furyl-ethyl)-phthalimide 
• 151-50-8 potassium cyanide 
• 58052-80-5 2,4,6-Trimethyl-[1,3,5]triazinane; hydrate 
• 17496-08-1 ammonium propionate 
• 74-90-8 hydrogen cyanide 
• 75-07-0 acetaldehyde 
• 623-11-0 1-methyl-4-nitrosobenzene 
• 127-17-3 2-oxo-propionic acid 
• 56-40-6 glycine 
• 59-51-8 DL-methionine 
• 67-64-1 acetone 

Downstream Products

• 75-07-0 acetaldehyde 
• 109454-92-4 N-(quinoline-2-carbonyl)-DL-alanine 
• 66789-75-1 N-[(2,4,5-trichloro-phenoxy)-acetyl]-L-alanine 
• 56777-63-0 N-(4-phenylazo-phenylcarbamoyl)-l-alanine 
• 114998-56-0 N-[(2,4,5-trichloro-phenoxy)-acetyl]-D-alanine 
• 99945-09-2 N-[(2,4-dichloro-phenoxy)-acetyl]-D-alanine 
• 100016-90-8 N-benzylsulfanylcarbonyl-DL-alanine 
• 99630-04-3 2-(4-bromo-2-nitrophenylamino)propionic acid 
• 114998-57-1 N-[(2,4,5-trichloro-phenoxy)-acetyl]-DL-alanine 
• 23446-00-6 N-(N-benzyloxycarbonyl-glycyl)-DL-alanine 
• 99548-52-4 2-(5-bromo-2-nitrophenylamino)propionic acid 
• 4815-91-2 N-phenylthioacetyl-alanine 
• 24639-11-0 N-hippuroyl-alanine 
• 63250-94-2 N-(N-benzyloxycarbonyl-β-alanyl)-alanine 

Relevant articles and documents

Synthesis and Reaction of a New Chiral Pyridoxamine Analogue; Some Doubt about the Stereochemical Process Tentatively Proposed for a Nonenzymatic Transamination Reaction

A pyridoxamine analogue-like chiral pyridinophane with two sulfonyl groups in the bridging chain, (S)-15-aminomethyl-14-hydroxy-2,8-dithia(2,5)pyridinophane S,S,S',S'-tetraoxide ((S)-7), was prepared by oxidation of the sulfide precursor, (S)-2.The amino group was successfully transferred from (S)-7 to several 2-oxo carboxylic acids in methanol at room temperature in the presence of one-half equimolecular zinc(II) ion, giving (R)-amino acids in excess.The reaction rates of this nonenzymatic transamination using chiral (S)-7 were much smaller than those of the corresponding reaction using chiral (S)-2.The enantiomeric excess of the amino acids obtained through the reactions of (S)-7 was compared with those of (S)-2, showing that (S)-7-was more efficient than (S)-2 for the preparation of (R)-alanine, but was less than that of (S)-2 for the preparations of (R)-valine, (R)-leucine, and (R)-phenylalanine.These results aroused some doubt about the previous explanation of the stereochemical features of such nonenzymatic transamination reactions.

The radiation-induced "hydrolysis" of the peptide boned.

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Real-time monitoring of D-Ala-D-Ala dipeptidase activity of VanX in living bacteria by isothermal titration calorimetry

The D,D-dipeptidase enzyme VanX is the main cause of vancomycin resistance in gram-positive bacteria because of hydrolysis of the D-Ala-D-Ala dipeptide used in cell-wall biosynthesis. Continuous assay of VanX has proven challenging due to lack of a chromophoric substrate. Here, we report a direct approach for continuous assay of VanX in vitro and in vivo from hydrolysis of D-Ala-D-Ala, based on the heat-rate changes measured with isothermal titration calorimetry (ITC). With the ITC approach, determination of kinetic parameters of VanX hydrolyzing D-Ala-D-Ala and the inhibition constant of D-cysteine inhibitor yielded KM of 0.10 mM, kcat of 11.5 s?1, and Ki of 18.8 μM, which are consistent with the data from ninhydrin/Cd(II)assays. Cell-based ITC studies demonstrated that the VanX expressed in E. coli and in clinical strain VRE was inhibited by D-cysteine with IC50 values of 29.8 and 28.6 μM, respectively. Also, the total heat from D-Ala-D-Ala (4 mM)hydrolysis decreases strongly (in absolute value)from 1.26 mJ for VRE to 0.031 mJ for E. faecalis, which is consistent with the large MIC value of vancomycin of 512 μg/mL for VRE and the much smaller value of 4 μg/mL for E. faecalis. The ITC approach proposed here could be applied to screen and evaluate small molecule inhibitors of VanX or to identify drug resistant bacteria.

Hydrolysis of acetyl-methionine-containing dipeptides promoted by palladium(II) complexes containing methionine-amino acids as ligands

The [Pd(N,S-Met-a'a'H)(N,S-AcMet-aaH)] (a'a'H and aaH = amino acids) was characterized by electrospray ionization mass spectrometer(ESI-MS) and 1H NMR, in which Met-a'a'H, as ligand, coordinates to Pd(II) via thioether and terminal amino group, and AcMet-aaH, as substrate, coordinates to Pd(II) via thioether and deprotonated amide nitrogen of methionine. The Met-a'a' bond in ligand is intact, the Met-aa bond in substrate, however, is activated toward hydrolysis The difference in hydrolysis behavior between ligand and substrate may be due to a fused six-membered and five-membered ring formation via thioether, deprotonated amide nitrogen and carbonyl oxygen of methionine residue in substrate.

Sinefungin VA and dehydrosinefungin V, new antitrypanosomal antibiotics produced by Streptomyces sp. K05-0178

Two new nucleotide antibiotics, named sinefungin VA and dehydrosinefungin V, were separated by cation exchange column chromatography and purified by HPLC from the culture broth of Streptomyces sp. K05-0178, together with the known antibiotics, sinefungin, dehydrosinefungin and KSA-9342. The structures of the two novel sinefungin analogs were elucidated by spectroscopic studies, including various NMR and advanced peptide chemical methods. Sinefungin VA consists of adenosine and ornithylvalylalanine, whereas dehydrosinefungin V consists of 4′,5′-dehydroadenosine and ornithylvaline. Sinefungin VA showed potent antitrypanosomal activity with an IC50 value of 0.0026 g ml 1 in vitro without cytotoxicity against MRC-5 cells. Dehydrosinefungin V showed moderate antitrypanosomal activity (IC50=0.15 μg ml-1).

Intramolecular Cyclization of the Pyridoxal-Histidine Schiff Base Controlled in Reversed Micelles

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Argifin, a new chitinase inhibitor, produced by Gliocladium sp. FTD-0668 II. Isolation, physico-chemical properties, and structure elucidation

A new chitinase inhibitor, named argifin, was isolated from the cultured broth of a fungal strain Gliocladium sp. FTD-0668. Argifin was purified from the cultured mycelium by the combination of cation exchange, anion exchange, adsorption, and gel filtration Chromatographie methods. The structure of argifin was elucidated as cyclo(N-(β-methylcarbamoyl)-L-arginylN-methyl-L-phenyIalanyl-β-L- aspartyl-β-L-aspartyl-D-alanyl) by NMR experiments and other spectroscopic analyses.

Artificial metalloenzymes based on protein cavities: Exploring the effect of altering the metal ligand attachment position by site directed mutagenesis

In an effort to construct catalysts with enzyme-like properties, we are employing a small, cavity-containing protein as a scaffold for the attachment of catalytic groups. In earlier work we demonstrated that a phenanthroline ligand could be introduced into the cavity of the protein ALBP and used to catalyze ester hydrolysis. To examine the effect of positioning the phenanthroline catalyst at different locations within the protein cavity, three new constucts - Phen60, Phen72 and Phen104 - were prepared. Each new conjugate was characterized by UV/vis spectroscopy, fluorescence spectroscopy, guanidine hydrochloride denaturation, gel filtration chromatography, and CD spectroscopy to confirm the preparation of the desired contruct. Analysis of reactions containing Ala-OiPr showed that Phen60 catalyzed ester hydrolysis with less selectivity than ALBP-Phen while Phen72 promoted this same reaction with higher selectivity. Reactions with Tyr-OMe were catalyzed with higher selectivity by Phen60 and more rapidly by Phen104. These results demonstrate that both the rates and selectivities of hydrolysis reactions catalyzed by these constructs are dependent on the precise site of attachment of the metal ligand within the protein cavity.

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Asymmetric electrosynthesis of amino acid using an electrode modified with amino acid oxidase and electron mediator

Asymmetric synthesis of amino acid has been successfully achieved by electrochemical reduction of keto acid using an electrode on which amino acid oxidase and electron mediator are immobilized. The enantiomer excess closing to 100% was obtained.

A potent polymer/pyridoxamine enzyme mimic

An enzyme mimic consisting of pyridoxamines covalently linked to polyethyleneimine carrying long-chain alkyl groups converts pyruvic acid to dl-alanine with as much as an 8000-fold acceleration relative to the reaction with simple pyridoxamine at the same pyridoxamine concentration. The acceleration by polymer is a strong function of the length of the alkyl chains that are appended. The polymer furnishes acid and base groups to catalyze the proton transfers that are involved in transamination. Copyright

Study of relaxation rates of stable paramagnetic centers in gamma-irradiated alanine.

The stable L-alanine radical induced by gamma-irradiation was examined by electron paramagnetic resonance (EPR), transfer saturation EPR and electron nuclear double resonance (ENDOR) in the temperature region of fast motion of the methyl group (180-320 K). From the obtained spectral line broadening and spectral intensity the correlation time for the methyl rotation was estimated. The complex processes determining the relaxation rate were examined in the same temperature interval. It was shown that important contributions to the relaxation rate arise from non-secular and pseudo-secular types of contributions. The non-secular contribution involves intramolecular dynamics while the pseudo-secular contribution originates from intermolecular motions. The obtained values for the dynamical parameters have been compared with those obtained by pulse EPR methods and by proton nuclear magnetic resonance (NMR) on undamaged crystals.

Asymmetric synthesis of α-amino acids using chiral cobalt(III) complexes

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Chiral Metal–Organic Framework Hollow Nanospheres for High-Efficiency Enantiomer Separation

Chiral ZIF-8 hollow nanospheres with d-histidine as part of chiral ligands (denoted as H-d-his-ZIF-8) were prepared for separation of (±)-amine acids. Compared to bulk d-his-ZIF-8 without a hollow cavity, the prepared H-d-his-ZIF-8 showed 15 times higher separation capacity and higher ee values of 90.5 % for alanine, 95.2 % for glutamic acid and 92.6 % for lysine, respectively.

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Thermodynamical characteristics of the reaction of pyridoxal-5'-phosphate with L-amino acids in aqueous buffer solution

The reaction of pyridoxal-5'-phosphate with L-isomers of alanine, lysine, arginine, aspartic acid, glutamic acid, and glycine in phosphate buffer solution was studied by absorption spectroscopy and the calorimetry of dissolution at physiological acidity of the medium (pH 7.35). The formation constants of Schiff bases during reactions and changes in Gibbs energy, enthalpy, and entropy were determined. It was shown that the formation constant of the Schiff base and its spectral properties depend on the nature of the bound amino acid. The progress of the reaction with a majority of amino acids is governed by the entropy factor due to the predominant role of the dehydration effect of the reaction center of amino acids during chemical reactions. The intramolecular electrostatic interaction of an ionized phosphate group with the positively charged amino group on the end of the chain of amino acid residue stabilizes the Schiff bases formed by lysine and arginine. The extinction coefficient of the base, equilibrium constant, and the exothermic effect of the reaction then increase. The excess negative charge on the end of the chain of amino acid residues of aspartic and glutamic acids destabilizes the molecule of the Schiff base. In this case, the equilibrium constant decreases and the endothermic effect of the reaction increases. Pleiades Publishing, Ltd., 2011.

Diketopiperazine-Type Alkaloids from a Deep-Sea-Derived Aspergillus puniceus Fungus and Their Effects on Liver X Receptor α

Eight new diketopiperazine-type alkaloids including four oxepin-containing diketopiperazine-type alkaloids, oxepinamides H-K (1-4), and four 4-quinazolinone alkaloids, puniceloids A-D (5-8), together with two known analogues (9 and 10), were isolated from the culture broth extracts of the deep-sea-derived fungus Aspergillus puniceus SCSIO z021. Their structures were elucidated by spectroscopic analyses, and their absolute configurations were determined by Marfey's method along with comparison of their specific rotations and ECD spectra. The absolute configurations of 4 and 5 were further confirmed by a single-crystal X-ray diffraction analysis. Compounds 1-8 showed significant transcriptional activation of liver X receptor α with EC50 values of 1.7-50 μM, and 7 and 8 were the most potent agonists.

Zelkovamycins B-E, Cyclic Octapeptides Containing Rare Amino Acid Residues from an Endophytic Kitasatospora sp

Four unusual cyclopeptides, zelkovamycins B-E (1-4), were isolated from an endophytic Kitasatospora sp. Zelkovamycin B was featured by an unprecedented 3-methyl-5-hydroxypyrrolidine-2,4-dione ring system linked to the cyclopeptide skeleton. Their structures and full configurations were established by spectroscopic analysis, Marfey's method, and NMR calculations. A plausible biosynthetic pathway for zelkovamycins was proposed based on gene cluster analysis. Zelkovamycin E displayed potent inhibitory activity against H1N1 influenza A virus.

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A one-pot enantioselective chemo-enzymatic synthesis of amino acids in water

The combination of immobilised Rh-Mono-Phos (1-AlTUD-1) and acylase I afforded a chemoenzymatic, one-pot process for the enantioselective synthesis of amino acids in water, without the need for isolation of intermediates. In addition, the enzymatic hydrolysis increases the enantiopurity of the product from 95% ee to >98% ee. Compatibility studies revealed that for optimum results compartmentalisation of the catalysts is required.

H2-Driven biocatalytic hydrogenation in continuous flow using enzyme-modified carbon nanotube columns

We describe the implementation of a system of immobilised enzymes for H2-driven NADH recycling coupled to a selective biotransformation to enable H2-driven biocatalysis in flow. This approach represents a platform that can be optimised for a wide range of hydrogenation steps and is shown here for enantioselective ketone reduction and reductive amination.

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Structural and functional highlights of methionine aminopeptidase 2 from Leishmania donovani

Methionine aminopeptidase 2 (MAP2) is a principal regulator of apoptosis for Leishmania donovani and a potential candidate for the design and synthesis of novel antileishmanials. The LdMAP2 gene was cloned in pET28a(+)-SUMO vector, expressed in E. coli and then purified by chromatographic methods. It was found to be a monomer and required divalent metal ion for its activity against synthetic substrates with Co(II), Mg(II), Mn(II) and Ni(II) being the major activators. Moreover, Ca(II) showed the tightest binding with Km value of 124.7 ± 9.2 μM, while Co(II) proved most efficient for catalysis with kcat value of 128.1 ± 4 min?1. The naturally occurring aminopeptidase B inhibitor bestatin was found to be a potent inhibitor of LdMAP2 with a Ki value of 0.86 μM. Further, structural studies with circular dichroism (CD) showed an increase in the α-helical and β-sheet contents and a decrease in random coils in LdMAP2 upon interactions with both bestatin and fluorogenic substrates. Finally, structural studies pointed out key differences in the structure of LdMAP2 and HsMAP2 and their interactions with inhibitor bestatin, Ala-AMC, Leu-AMC and Met-AMC. The structural differences of two orthologs and different binding modes with bestatin can be crucial for the development of novel and specific inhibitor against leishmaniasis.

Enzymatic characterization and crystal structure of biosynthetic alanine racemase from Pseudomonas aeruginosa PAO1

Alanine racemase is a pyridoxal-5′-phosphate (PLP)-dependent enzyme that reversibly catalyzes the conversion of L-alanine to D-alanine. D-alanine is an essential constituent in many prokaryotic cell structures. Inhibition of alanine racemase is lethal to prokaryotes, creating an attractive target for designing antibacterial drugs. Here we report the crystal structure of biosynthetic alanine racemase (Alr) from a pathogenic bacteria Pseudomonas aeruginosa PAO1. Structural studies showed that P. aeruginosa Alr (PaAlr) adopts a conserved homodimer structure. A guest substrate D-lysine was observed in the active site and refined to dual-conformation. Two buffer ions, malonate and acetate, were bound in the proximity to D-lysine. Biochemical characterization revealed the optimal reaction conditions for PaAlr.

Squamins C–F, four cyclopeptides from the seeds of Annona globiflora

Four cyclic octapeptides, squamins C–F, were isolated from the seeds of Annona globiflora Schltdl. These compounds share part of their amino acid sequence, -Pro-Met(O)-Tyr-Gly-Thr-, with previously reported squamins A and B. Their structures were determined using NMR spectroscopic techniques together with quantum mechanical calculations (QM-NMR), ESI-HRMS data and a modified version of Marfey's chromatographic method. All compounds showed cytotoxic activity against DU-145 (human prostate cancer) and HeLa (human cervical carcinoma) cell lines. Clearly, A. globiflora is an important source of bioactive molecules, which could promote the sustainable exploitation of this undervalued specie.

Biosynthesis ofl-alanine fromcis-butenedioic anhydride catalyzed by a triple-enzyme cascadeviaa genetically modified strain

In industry,l-alanine is biosynthesized using fermentation methods or catalyzed froml-aspartic acid by aspartate β-decarboxylase (ASD). In this study, a triple-enzyme system was developed to biosynthesizel-alanine fromcis-butenedioic anhydride, which was cost-efficient and could overcome the shortcomings of fermentation. Maleic acid formed bycis-butenedioic anhydride dissolving in water was transformed tol-alanineviafumaric acid andl-asparagic acid catalyzed by maleate isomerase (MaiA), aspartase (AspA) and ASD, respectively. The enzymatic properties of ASD from different origins were investigated and compared, as ASD was the key enzyme of the triple-enzyme cascade. Based on cofactor dependence and cooperation with the other two enzymes, a suitable ASD was chosen. Two of the three enzymes, MaiA and ASD, were recombinant enzymes cloned into a dual-promoter plasmid for overexpression; another enzyme, AspA, was the genomic enzyme of the host cell, in which AspA was enhanced by a T7promoter. Two fumarases in the host cell genome were deleted to improve the utilization of the intermediate fumaric acid. The conversion of whole-cell catalysis achieved 94.9% in 6 h, and the productivity given in our system was 28.2 g (L h)?1, which was higher than the productivity that had been reported. A catalysis-extraction circulation process for the synthesis ofl-alanine was established based on high-density fermentation, and the wastewater generated by this process was less than 34% of that by the fermentation process. Our results not only established a new green manufacturing process forl-alanine production fromcis-butenedioic anhydride but also provided a promising strategy that could consider both catalytic ability and cell growth burden for multi-enzyme cascade catalysis.

Mechanistic insight into metal ion-catalyzed transamination

Several classes of biological reactions that are mediated by an enzyme and a co-factor can occur, to a slower extent, not only without the enzyme but even without the co-factor, under catalysis by metal ions. This observation has led to the proposal that metabolic pathways progressively evolved from using inorganic catalysts to using organocatalysts of increasing complexity. Transamination, the biological process by which ammonia is transferred between amino acids and α-keto acids, has a mechanism that has been well studied under enzyme/co-factor catalysis and under co-factor catalysis, but the metal ion-catalyzed variant was generally studied mostly at high temperatures (70-100 °C), and the details of its mechanism remained unclear. Here, we investigate which metal ions catalyze transamination under conditions relevant to biology (pH 7, 20-50 °C) and study the mechanism in detail. Cu2+, Ni2+, Co2+, and V5+ were identified as the most active metal ions under these constraints. Kinetic, stereochemical, and computational studies illuminate the mechanism of the reaction. Cu2+ and Co2+ are found to predominantly speed up the reaction by stabilizing a key imine intermediate. V5+ is found to accelerate the reaction by increasing the acidity of the bound imine. Ni2+ is found to do both to a limited extent. These results show that direct metal ion-catalyzed amino group transfer is highly favored even in the absence of co-factors or protein catalysts under biologically compatible reaction conditions.