L-Pyroglutamic acid-β-naphthylamide
Need Assistance?
  • US & Canada:
    +
  • UK: +

L-Pyroglutamic acid-β-naphthylamide

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

Substrate for the determination of pyrrolidonylpeptidase.

Category
Cyclic Amino Acids
Catalog number
BAT-005609
CAS number
22155-91-5
Molecular Formula
C15H14N2O2
Molecular Weight
254.3
L-Pyroglutamic acid-β-naphthylamide
IUPAC Name
(2S)-N-naphthalen-2-yl-5-oxopyrrolidine-2-carboxamide
Synonyms
L-Pyr-βNA
Appearance
White to off-white powder
Purity
≥ 99% (HPLC)
Density
1.311 g/cm3
Melting Point
188-193 °C
Boiling Point
616.9 ºC
Storage
Store at 2-8°C
InChI
InChI=1S/C15H14N2O2/c18-14-8-7-13(17-14)15(19)16-12-6-5-10-3-1-2-4-11(10)9-12/h1-6,9,13H,7-8H2,(H,16,19)(H,17,18)/t13-/m0/s1
InChI Key
BZEPQNMASTUAMY-ZDUSSCGKSA-N
Canonical SMILES
C1CC(=O)NC1C(=O)NC2=CC3=CC=CC=C3C=C2
1. Assay of tryptophan hydroxylase and aromatic L-amino acid decarboxylase based on rapid separation of the reaction product by high performance liquid chromatography
H Hasegawa, M Yanagisawa, A Ichiyama J Biochem. 1984 Jun;95(6):1751-8.
A rapid separation of 5-hydroxytryptophan by high performance liquid chromatography (HPLC) was achieved for the assay of tryptophan hydroxylase. "Bulk separation" of the product from all other components in the reaction mixture by HPLC was achieved by 1) the choice of a suitable column-solvent system so as to elute the reaction product ahead of other components in the sample mixture, 2) the use of a monitor selective for the reaction product, 3) minimization of the column length so as to achieve rapid separation of the product from the substrate. The method finally employed a reversed phase column of 5 cm length, relatively rapid elution at 2 ml/min and fluorescence detection at 350 nm with an excitation at 302 nm. The assay is convenient and as sensitive as the radioisotope method. The advantages of the method are 1) almost no pretreatment of samples, 2) repeatability every 2 min, 3) wide latitude of product determination from picomole to nanomole amounts per assay. The method was extended to the assay of 5-hydroxytryptophan decarboxylase by essentially the same procedures.
2. Continuous spectrometric assays for glutaminyl cyclase activity
Stephan Schilling, Torsten Hoffmann, Michael Wermann, Ulrich Heiser, Claus Wasternack, Hans-Ulrich Demuth Anal Biochem. 2002 Apr 1;303(1):49-56. doi: 10.1006/abio.2001.5560.
The enzymatic conversion of one chromogenic substrate, l-glutamine-p-nitroanilide, and two fluorogenic substrates, l-glutaminyl-2-naphthylamide and l-glutaminyl-4-methylcoumarinylamide, into their respective pyroglutamic acid derivatives by glutaminyl cyclase (QC) was estimated by introducing a new coupled assay using pyroglutamyl aminopeptidase as the auxiliary enzyme. For the purified papaya QC, the kinetic parameters were found to be in the range of those previously reported for other glutaminyl peptides, such as Gln-Gln, Gln-Ala, or Gln-tert-butyl ester. The assay can be performed in the presence of ammonia up to a concentration of 50 mM. Increasing ionic strength, e.g., potassium chloride up to 300 mM, resulted in an increase in enzymatic activity of about 20%. This is the first report of a fast, continuous, and reliable determination of QC activity, even in the presence of ammonium ions, during the course of protein purification and enzymatic analysis.
3. A fluorometric assay for measuring deamidase (lysosomal protective protein) using high-performance liquid chromatography
T Chikuma, K Matsumoto, A Furukawa, N Nakayama, R Yajima, T Kato, Y Ishii, A Tanaka Anal Biochem. 1996 Jan 1;233(1):36-41. doi: 10.1006/abio.1996.0004.
A rapid and sensitive assay method for the determination of deamidase activity is reported. This method is based on fluorometric detection of a dansylated dipeptide, 5-dimethylaminonaphthalene-1-sulfonyl-D-Tyr-Val (N-Dns-D-Tyr-Val), enzymatically formed from the substrate 5-dimethylaminonaphthalene-1-sulfonyl-D-Tyr-Val-NH2 (N-Dns-D-Tyr-Val-NH2), after separation by high-performance liquid chromatography (HPLC) using a C-18 reversed-phase column by isocratic elution. This method is sensitive enough to measure N-Dns-D-Tyr-Val at concentrations as low as 100 fmol, yields highly reproducible results and requires less than 8.5 min per sample for separation and quantitation. The optimum pH for deamidase activity was 4.0-4.5. Greater than 5 mM of reduced glutathione was needed for maximal enzyme activity. The Km and Vmax values were respectively 125 microM and 14.12 pmol/micrograms/h with the use of enzyme extract obtained from mouse spleen. Deamidase activity was strongly inhibited by Ag+, Cu2+, diisopropylfluorophosphate, and p-chloromercuriphenylsulfonic acid. Among the organs examined in a mouse, the highest specific activity of the enzyme was found in spleen. The sensitivity and selectivity of this method will aid in efforts to examine the physiological role of this enzyme.
Online Inquiry
Verification code
Inquiry Basket