L-Phenylalanine 4-nitroanilide
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L-Phenylalanine 4-nitroanilide

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A substrate for aminopeptidase M (microsomal alanyl aminopeptidase).

Category
L-Amino Acids
Catalog number
BAT-004015
CAS number
2360-97-6
Molecular Formula
C15H15N3O3
Molecular Weight
285.30
L-Phenylalanine 4-nitroanilide
IUPAC Name
(2S)-2-amino-N-(4-nitrophenyl)-3-phenylpropanamide
Synonyms
L-Phe-pNA; L-phenylalanine N-(4-nitrophenyl)amide; H-Phe-pNA; L-phenylalanine p-nitroanilide; (S)-2-Amino-N-(4-nitrophenyl)-3-phenylpropanamide
Appearance
Light yellow powder
Purity
≥ 99% (HPLC)
Density
1.323 g/cm3
Melting Point
149-155 °C
Boiling Point
543.0 °C at 760 mmHg
Storage
Store at 2-8 °C
InChI
InChI=1S/C15H15N3O3/c16-14(10-11-4-2-1-3-5-11)15(19)17-12-6-8-13(9-7-12)18(20)21/h1-9,14H,10,16H2,(H,17,19)/t14-/m0/s1
InChI Key
GJHIOWXZFDVUKQ-AWEZNQCLSA-N
Canonical SMILES
C1=CC=C(C=C1)CC(C(=O)NC2=CC=C(C=C2)[N+](=O)[O-])N
1. Kinetics of N-glutaryl-L-phenylalanine p-nitroanilide hydrolysis catalyzed by alpha-chymotrypsin in aqueous solutions of dodecyltrimethylammonium bromide
Elsa Abuin, Eduardo Lissi, Roxanna Duarte J Colloid Interface Sci. 2005 Mar 15;283(2):539-43. doi: 10.1016/j.jcis.2004.08.177.
The rate of hydrolysis of N-glutaryl-L-phenylalanine p-nitroanilide (GPNA) catalyzed by alpha-chymotrypsin (alpha-CT) has been measured in aqueous solutions of dodecyltrimethylammonium bromide (DTAB) at concentrations below and above the critical micelle concentration, as well as in the absence of surfactant. Under all the conditions employed, the reaction follows a Michaelis-Menten mechanism. The presence of the surfactant leads to superactivity below and above the critical micelle concentration (CMC), with a maximum reaction rate taking place near the CMC when the results are treated in terms of the analytical concentration of the substrate. A similar behavior was observed by working with the enzyme partially deactivated in the presence of 4 M urea. After correction to take into account the partitioning of the substrate between the micelles and the external media, the activity of the enzyme tends to remain almost constant above the corresponding CMCs. This results from a compensation of a decrease in the catalytic constant (k(cat)) and a decrease in the Michaelis constant (K(M)). The behavior of alpha-CT in the hydrolysis of GPNA in DTAB solutions is at variance with that previously reported for the hydrolysis of 2-naphthyl acetate in solutions of the same surfactant (E. Abuin, E. Lissi, R. Duarte, Langmuir 19 (2003) 5374). An explanation of the different effects of the surfactant on the behavior of the enzyme with both substrates is advanced, taking into account the complexity of the mechanism of the alpha-CT-mediated reaction, more specifically, in terms of different rate-limiting steps for the formation of the measured products.
2. Enzymatic attack on immobilized substrates. 2. Diffusional limitations in the alpha-chymotrypsin-catalyzed hydrolysis of polyacrylamide-bound l-phenylalanine 4-nitroanilide
J Fischer, L Lange, H D Jakubke Eur J Biochem. 1978 Aug 1;88(2):453-7. doi: 10.1111/j.1432-1033.1978.tb12469.x.
1. The chymotrypsin-catalyzed hydrolysis of polyacrylamide-bound L-phenylalanine 4-nitroanilide was studied. As a spacer, one or two 6-aminohexanoyl residues were inserted between the matrix and ligand. 2. In the course of the enzymatic hydrolysis of polyacrylamide-bound substrates, enzyme adsorption by the gel substrates was observed. A quasi equilibrium of enzyme partitioning was reached after approximately 20-min incubation time. The enzyme adsorption could be described by the Langmuir adsorption isotherm. 3. The substrates attached via spacers to the matrix were completely hydrolyzed. 4. The initial course of the product vs time curves, as well as the dependence of the initial hydrolysis rates on enzyme concentration or substrate concentration, have been interpreted by the Nernst reaction theory. From the results obtained it has been concluded that the inital rate of the hydrolysis of polyacrylamide-bound L-phenylalanine 4-nitroanilide depends on the velocity of enzyme diffusion into the matrix.
3. L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide--a chromogenic substrate for thiol proteinase assay
Filippova IYu, E N Lysogorskaya, E S Oksenoit, G N Rudenskaya, V M Stepanov Anal Biochem. 1984 Dec;143(2):293-7. doi: 10.1016/0003-2697(84)90665-1.
L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide (PFLNA)--a convenient chromogenic substrate for assay of thiol proteinases papain, ficin, and bromelain--was prepared by enzymatic synthesis with chymotrypsin as a catalyst. The thiol proteinases hydrolyze PFLNA with the liberation of p-nitroaniline, estimated spectrophotometrically by its absorbance at 410 nm. The phenylalanine residue in the P2 position of PFLNA meets the specificity demands of thiol proteinases. The following values of Km were found for PFLNA hydrolysis: by papain, 0.34 mM; by ficin, 0.43 mM; by bromelain, 0.30 mM. This substrate was successfully applied to monitor thiol proteinase affinity chromatography on bacitracin-Sepharose, which resulted in a 2- to 4-fold purification from commercial preparations.
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