Nα-[2,4-Dinitro-5-fluorophenyl]-L-valine amide

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Nα-[2,4-Dinitro-5-fluorophenyl]-L-valine amide
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A derivatizing chiral agent that can be used for detection of underivatized amino acids in HPLC.

Fluorinated amino acids
Catalog number
CAS number
Molecular Formula
Molecular Weight
Nα-[2,4-Dinitro-5-fluorophenyl]-L-valine amide
FDNP-L-Val-NH2; (S)-2-((5-Fluoro-2,4-dinitrophenyl)amino)-3-methylbutanamide
Yellow powder
≥ 99 % (HPLC)
1.469 g/cm3
Boiling Point
537.5 ℃ at 760 mmHg
Store at 2-8 ℃
InChI Key
Canonical SMILES
1. Exploring Peptide Ligase Orthologs in Actinobacteria-Discovery of Pseudopeptide Natural Products, Ketomemicins
Yasushi Ogasawara, Junpei Kawata, Motoyoshi Noike, Yasuharu Satoh, Kazuo Furihata, Tohru Dairi ACS Chem Biol. 2016 Jun 17;11(6):1686-92. doi: 10.1021/acschembio.6b00046. Epub 2016 Apr 8.
We recently identified a novel peptide ligase (PGM1), an ATP-grasp-ligase, that catalyzes amide bond formation between (S)-2-(3,5-dihydroxy-4-methoxyphenyl)-2-guanidinoacetic acid and ribosomally supplied oligopeptides in pheganomycin biosynthesis. This was the first example of an ATP-grasp-ligase utilizing peptides as nucleophiles. To explore the potential of this type of enzyme, we performed a BLAST search and identified many orthologs. The orthologs of Streptomyces mobaraensis, Salinispora tropica, and Micromonospora sp. were found in similar gene clusters consisting of six genes. To probe the functions of these genes, we heterologously expressed each of the clusters in Streptomyces lividans and detected novel and structurally similar pseudotripeptides in the broth of all transformants. Moreover, a recombinant PGM1 ortholog of Micromonospora sp. was demonstrated to be a novel dipeptide ligase catalyzing amide bond formation between amidino-arginine and dipeptides to yield tripeptides; this is the first report of a peptide ligase utilizing dipeptides as nucleophiles.
2. A novel prokaryotic L-arginine:glycine amidinotransferase is involved in cylindrospermopsin biosynthesis
Julia Muenchhoff, Khawar S Siddiqui, Anne Poljak, Mark J Raftery, Kevin D Barrow, Brett A Neilan FEBS J. 2010 Sep;277(18):3844-60. doi: 10.1111/j.1742-4658.2010.07788.x. Epub 2010 Aug 16.
We report the first characterization of an L-arginine:glycine amidinotransferase from a prokaryote. The enzyme, CyrA, is involved in the pathway for biosynthesis of the polyketide-derived hepatotoxin cylindrospermopsin from Cylindrospermopsis raciborskii AWT205. CyrA is phylogenetically distinct from other amidinotransferases, and structural alignment shows differences between the active site residues of CyrA and the well-characterized human L-arginine:glycine amidinotransferase (AGAT). Overexpression of recombinant CyrA in Escherichia coli enabled biochemical characterization of the enzyme, and we confirmed the predicted function of CyrA as an L-arginine:glycine amidinotransferase by (1) H NMR. As compared with AGAT, CyrA showed narrow substrate specificity when presented with substrate analogs, and deviated from regular Michaelis-Menten kinetics in the presence of the non-natural substrate hydroxylamine. Studies of initial reaction velocities and product inhibition, and identification of intermediate reaction products, were used to probe the kinetic mechanism of CyrA, which is best described as a hybrid of ping-pong and sequential mechanisms. Differences in the active site residues of CyrA and AGAT are discussed in relation to the different properties of both enzymes. The enzyme had maximum activity and maximum stability at pH 8.5 and 6.5, respectively, and an optimum temperature of 32 °C. Investigations into the stability of the enzyme revealed that an inactivated form of this enzyme retained an appreciable amount of secondary structure elements even on heating to 94 °C, but lost its tertiary structure at low temperature (T(max) of 44.5 °C), resulting in a state reminiscent of a molten globule. CyrA represents a novel group of prokaryotic amidinotransferases that utilize arginine and glycine as substrates with a complex kinetic mechanism and substrate specificity that differs from that of the eukaryotic L-arginine:glycine amidinotransferases.
3. Structure and reaction mechanism of L-arginine:glycine amidinotransferase
A Humm, E Fritsche, S Steinbacher Biol Chem. 1997 Mar-Apr;378(3-4):193-7.
L-Arginine:glycine amidinotransferase (AT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the direct precursor of creatine. The X-ray structure of the human enzyme shows a novel fold with fivefold pseudosymmetry of beta beta alphabeta-modules. These modules enclose the active site compartment of the basket-like structure. The active site of AT lies at the bottom of a very narrow channel and contains a catalytic triad with the residues Cys-His-Asp. The transamidination reaction follows a ping-pong mechanism and is accompanied by large conformational changes. During catalysis the amidino group is covalently attached to the active site cysteine to give an amidino-cysteine intermediate.

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