Unfortunately, no data indicating whether L7002 L-Lysine p-nitroanilide dihydrobromide might be a suitable substrate for the enzyme is collected. A search of the BRENDA enzyme database mentioned N-p-tosyl-Gly-Pro-Lys-4-nitroanilide but provided no evidence that L-Lysine p-nitroanilide is a substrate.
L7002
L-Lysine p-nitroanilide dihydrobromide
≥98% (TLC), suitable for ligand binding assays
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About This Item
Empirical Formula (Hill Notation):
C12H18N4O3 · 2HBr
CAS Number:
Molecular Weight:
428.12
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
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Product Name
L-Lysine p-nitroanilide dihydrobromide,
assay
≥98% (TLC)
Quality Level
form
powder
technique(s)
ligand binding assay: suitable
color
white to off-white
storage temp.
2-8°C
SMILES string
Br.NCCCC[C@H](N)C(=O)Nc1ccc(cc1)N(=O)=O
InChI
1S/C12H18N4O3.BrH/c13-8-2-1-3-11(14)12(17)15-9-4-6-10(7-5-9)16(18)19;/h4-7,11H,1-3,8,13-14H2,(H,15,17);1H/t11-;/m0./s1
InChI key
FJNCJWJSSUJZMS-MERQFXBCSA-N
1 of 4
This Item | A2010 | A6376 | C3647 |
|---|---|---|---|
| form powder | form powder | form powder | form powder |
| assay ≥98% (TLC) | assay ≥98% (TLC) | assay ≥99% (TLC) | assay ≥98% (TLC) |
| technique(s) ligand binding assay: suitable | technique(s) ligand binding assay: suitable | technique(s) ligand binding assay: suitable | technique(s) ligand binding assay: suitable |
| storage temp. 2-8°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C |
| color white to off-white | color colorless to white | color white to off-white | color white |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
Application
L-Lysine p-nitroanilide may be used as a substrate to study the specificity and kinetics of lysine aminopeptidase(s) and various proteinases.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Akifumi Kawamura et al.
Biomacromolecules, 6(2), 627-631 (2005-03-15)
The amidase activity of bovine pancreas trypsin in water-soluble complexes with poly(ethylene glycol)-block-poly(alpha,beta-aspartic acid) (PEG-PAA) was evaluated by a colorimetric assay using L-lysine p-nitroanilide as a substrate. The enzymatic reaction of trypsin was accelerated through the complexation with PEG-PAA. By
Natasa Bozić et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 134(2), 231-241 (2003-02-06)
Exopeptidases of Morimus funereus larvae were partially purified and characterized. Specific leucyl aminopeptidase (LAP) activity was increased eight-fold by gel filtration of the crude midgut extract. The partially purified LAP had a molecular mass greater than 100 kDa with pH
Bernardo Ramírez-Zavala et al.
FEMS microbiology letters, 235(2), 369-375 (2004-06-09)
A lysine aminopeptidase was purified from the yeast Kluyveromyces marxianus. This enzyme was purified 100-fold from a soluble extract obtained at 100,000g. The purification procedure consisted in fractionated precipitation with ammonium sulfate and five chromatography steps. The native enzyme had
Priscilla L Phillips et al.
PloS one, 13(11), e0207295-e0207295 (2018-11-13)
The oral obligate anaerobe Porphyromonas gingivalis possesses a small conserved transcript PG_RS02100 of unknown function we previously identified using small RNA-seq analysis as expressed during logarithmic growth. In this study, we sought to determine if PG_RS02100 plays a role in
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Can we use L-Lysine p-nitroanilide dihydrobromide as a substrate for enzyme assay of lysine gingipain protease?
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