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

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Category
L-Amino Acids
Catalog number
BAT-007806
CAS number
161513-46-8
Molecular Formula
C12H12N2O2
Molecular Weight
216.24
3-(2'-Quinolyl)-L-alanine
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
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.
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