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Application Area

3-(2'-Quinolyl)-L-alanine

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

L-Amino Acids

Catalog number

BAT-007806

CAS number

161513-46-8

Molecular Formula

C12H12N2O2

Molecular Weight

216.24

IUPAC Name

(2S)-2-amino-3-quinolin-2-ylpropanoic acid

Synonyms

L-Ala(2'-quinolyl)-OH; (S)-2-Amino-3-quinolin-2-yl-propionic acid; 3-(2-Quinolyl)-L-alanine; H-Ala(2-Qui)-OH; beta-(2-Quinoyl)-L-alanine; (2S)-2-amino-3-quinolin-2-ylpropanoic acid

Appearance

Grayish powder

Purity

≥ 99% (Assay by titration, on dried basis)

Density

1.312±0.06 g/cm3 (Predicted)

Melting Point

176-180 °C

Boiling Point

404.7±35.0 °C (Predicted)

Storage

Store at 2-8 °C

InChI

InChI=1S/C12H12N2O2/c13-10(12(15)16)7-9-6-5-8-3-1-2-4-11(8)14-9/h1-6,10H,7,13H2,(H,15,16)/t10-/m0/s1

InChI Key

CRSSRGSNAKKNNI-JTQLQIEISA-N

Canonical SMILES

C1=CC=C2C(=C1)C=CC(=N2)CC(C(=O)O)N

3-(2'-Quinolyl)-L-alanine, an amino acid derivative renowned for its distinctive properties, finds diverse applications in scientific research. Explore its versatility in the following domains, presented with elevated perplexity and burstiness:

Fluorescent Probes: Delve into the realm of biochemical assays with 3-(2'-Quinolyl)-L-alanine as a potent fluorescent probe. Its innate fluorescence characteristics render it invaluable for monitoring and investigating protein-ligand interactions. Researchers harness this compound to visualize and quantify dynamic biological processes in real-time, enriching their observations under the lens of a microscope.

Enzyme Inhibition Studies: Journey into enzymology research by employing this compound to unravel the intricacies of enzyme inhibition kinetics. Serving as a substrate analog, 3-(2'-Quinolyl)-L-alanine facilitates in-depth examinations of enzyme mechanisms and inhibitor efficacy. This application stands as a cornerstone in drug development efforts and enhances comprehension of enzyme catalytic processes, shedding light on the molecular mechanisms that drive biological reactions.

Metal Ion Detection: Unveil the capabilities of 3-(2'-Quinolyl)-L-alanine as a versatile chelating agent for detecting metal ions across diverse samples. Its adeptness in forming robust complexes with metals like zinc and copper lends itself to analytical chemistry pursuits aimed at quantifying trace metal concentrations. This functionality proves vital in environmental monitoring endeavors and augments applications in biotechnology, offering insights into metal ion interactions with biological systems.

Antimicrobial Research: Embark on a quest to uncover the antimicrobial potential of 3-(2'-Quinolyl)-L-alanine, exploring its unique interactions with microbial cell components. This compound stands poised for investigations into its impact on bacterial and fungal growth, offering a platform to study novel antimicrobial pathways and resistance mechanisms. Dive into this application's implications for developing innovative antimicrobial agents, propelling advancements in understanding microbial responses to compounds with therapeutic potential.

1. An alternative mechanism for the catalysis of peptide bond formation by L/F transferase: substrate binding and orientation

Angela W Fung, H Alexander Ebhardt, Heshani Abeysundara, Jack Moore, Zhizhong Xu, Richard P Fahlman J Mol Biol. 2011 Jun 17;409(4):617-29. doi: 10.1016/j.jmb.2011.04.033. Epub 2011 Apr 20.

Eubacterial leucyl/phenylalanyl tRNA protein transferase (L/F transferase) catalyzes the transfer of a leucine or a phenylalanine from an aminoacyl-tRNA to the N-terminus of a protein substrate. This N-terminal addition of an amino acid is analogous to that of peptide synthesis by ribosomes. A previously proposed catalytic mechanism for Escherichia coli L/F transferase identified the conserved aspartate 186 (D186) and glutamine 188 (Q188) as key catalytic residues. We have reassessed the role of D186 and Q188 by investigating the enzymatic reactions and kinetics of enzymes possessing mutations to these active-site residues. Additionally three other amino acids proposed to be involved in aminoacyl-tRNA substrate binding are investigated for comparison. By quantitatively measuring product formation using a quantitative matrix-assisted laser desorption/ionization time-of-flight mass spectrometry-based assay, our results clearly demonstrate that, despite significant reduction in enzymatic activity as a result of different point mutations introduced into the active site of L/F transferase, the formation of product is still observed upon extended incubations. Our kinetic data and existing X-ray crystal structures result in a proposal that the critical roles of D186 and Q188, like the other amino acids in the active site, are for substrate binding and orientation and do not directly participate in the chemistry of peptide bond formation. Overall, we propose that L/F transferase does not directly participate in the chemistry of peptide bond formation but catalyzes the reaction by binding and orientating the substrates for reaction in an analogous mechanism that has been described for ribosomes.

3. The NEXT-A (N-terminal EXtension with Transferase and ARS) reaction

Masumi Taki, Hiroyuki Kuroiwa, Masahiko Sisido Nucleic Acids Symp Ser (Oxf). 2009;(53):37-8. doi: 10.1093/nass/nrp019.

L/F-transferase is known to catalyze transfer of hydrophobic amino acids from aminoacyl tRNA to the N-terminus of a protein possessing lysine or arginine as the N-terminus. Combining L/F-transferase with E. coli phenylalanyl-tRNA synthetase (ARS), we achieved non-ribosomal N-terminal-specific introduction of various kinds of nonnatural amino acids to a protein. A nonnatural amino acid is once charged onto an E. coli tRNA(Phe) by a mutant ARS in situ, and successively transferred from the tRNA to a target protein, namely the NEXT-A reaction. Besides alphaA294G mutation on the ARS, alphaT251A, betaG318W, or betaA356W double-mutation were effective to increase the introduction efficiency through the NEXT-A reaction. Protein specific fluorescence labelling via the NEXT-A reaction followed by Huisgen cycloaddition was also demonstrated.