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Merck
CN

G2505

N-Glutaryl-L-phenylalanine p-nitroanilide

protease substrate

Synonym(s):

Glutaryl-L-phenylalanine 4-nitroanilide

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About This Item

Empirical Formula (Hill Notation):
C20H21N3O6
CAS Number:
5800-34-0
Molecular Weight:
399.40
UNSPSC Code:
12352204
NACRES:
NA.83
PubChem Substance ID:
24895096
EC Number:
227-351-4
Beilstein/REAXYS Number:
2919832
MDL number:
MFCD00038362

Key Documents

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InChI key

LFZGBNATHRHOKZ-KRWDZBQOSA-N

InChI

1S/C20H21N3O6/c24-18(7-4-8-19(25)26)22-17(13-14-5-2-1-3-6-14)20(27)21-15-9-11-16(12-10-15)23(28)29/h1-3,5-6,9-12,17H,4,7-8,13H2,(H,21,27)(H,22,24)(H,25,26)/t17-/m0/s1

SMILES string

OC(=O)CCCC(=O)N[C@@H](Cc1ccccc1)C(=O)Nc2ccc(cc2)[N+]([O-])=O

assay

≥98% (HPLC)

form

powder

solubility

methanol with 1 M NH4OH: 50 mg/mL, clear to slightly hazy

storage temp.

−20°C

Quality Level

100

Application

N-Glutaryl-L-phenylalanine p-nitroanilide has been used as a substrate to determine chymotrypsin activity.

Biochem/physiol Actions

N-Glutaryl-L-phenylalanine p-nitroanilide is useful in testing α-chymotrypsin activity.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
MKCZ4284
MKCX5416
MKCX0556
MKCR1562
MKCR0464

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New properties of chymotrypsin modified by fixation with a hydrophobic molecule: hexanal.
M H Remy et al.
Annals of the New York Academy of Sciences, 434, 343-346 (1984-01-01)
Daniel Brugger et al.
The British journal of nutrition, 116(3), 425-433 (2016-05-28)
This study investigated the effects of short-term subclinical Zn deficiency on exocrine pancreatic activity and changes in digestive capacity. A total of forty-eight weaned piglets were fed ad libitum a basal diet (maize and soyabean meal) with adequate Zn supply
S V Verevka
Ukrainskii biokhimicheskii zhurnal (1978), 68(3), 36-41 (1996-05-01)
Data on the kinetics of S2'-stimulated alpha-chymotrypsin action have been presented. It is supposed that the increase of the catalytic action of S2'-stimulated chymotrypsin occurs at all three stages of the hydrolytic process-at the enzyme-substrate complex formation, its transformation to
S Blais et al.
The Journal of biological chemistry, 268(25), 18637-18639 (1993-09-05)
The Michaelis constant of alpha-chymotrypsin, immobilized on a glutaraldehyde-activated silicate support, for N-glutaryl-L-phenylalanine-p-nitroanilide was determined and was found to be identical with that of the enzyme in solution. The influence of intraparticular diffusion was taken into account by immobilizing different
N Spreti et al.
European journal of biochemistry, 268(24), 6491-6497 (2001-12-12)
alpha-Chymotrypsin activity was tested with N-glutaryl-l-phenylalanine p-nitroanilide (GPNA) in aqueous media in the presence of synthetic surfactants, which differ in the flexibility of their bulky head groups. Superactivity can be ascribed to the presence of the tributylammonium residue on the
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