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S7632

Sigma-Aldrich

N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide

protease substrate

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About This Item

Empirical Formula (Hill Notation):
C24H34N6O9
CAS Number:
Molecular Weight:
550.56
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

assay

≥98% (TLC)

form

powder

solubility

DMF: 10 mg/mL, clear, colorless

UniProt accession no.

storage temp.

−20°C

SMILES string

CC(C)C(NC(=O)C(C)NC(=O)C(C)NC(=O)CCC(O)=O)C(=O)NC(C)C(=O)Nc1ccc(cc1)N(=O)=O

InChI

1S/C24H34N6O9/c1-12(2)20(24(37)27-14(4)22(35)28-16-6-8-17(9-7-16)30(38)39)29-23(36)15(5)26-21(34)13(3)25-18(31)10-11-19(32)33/h6-9,12-15,20H,10-11H2,1-5H3,(H,25,31)(H,26,34)(H,27,37)(H,28,35)(H,29,36)(H,32,33)

InChI key

IYHHIHIBYVIDMJ-UHFFFAOYSA-N

Gene Information

mouse ... Npy(109648)

General description

N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide is a chromogenic and a synthetic peptide substrate for proteases, elastase and subtilisin.

Application

N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide has been used as a synthetic peptide substrate for:
  • Bacillus pumilus alkaline protease (DHAP)
  • mesophilic subtilisin Carlsberg (sC) to assess the hydrolytic activity of wild-type and mutant sC
  • Pseudoalteromonas arctica cold-active protease (Pro21717)

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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Min-Yuan Wan et al.
Applied biochemistry and biotechnology, 159(2), 394-403 (2009-01-10)
An alkaline protease (DHAP) from Bacillus pumilus has shown great potential in hide dehairing. To get better insights on its catalytic properties for application, the substrate specificity and thermostability were investigated using five natural proteins and nine synthetic peptides. The
Ha Ju Park et al.
PloS one, 13(2), e0191740-e0191740 (2018-02-22)
Enzymes isolated from organisms found in cold habitats generally exhibit higher catalytic activity at low temperatures than their mesophilic homologs and are therefore known as cold-active enzymes. Cold-active proteases are very useful in a variety of biotechnological applications, particularly as
Naoki Fuchita et al.
Biochimica et biophysica acta, 1824(4), 620-626 (2012-02-14)
A comparison of the primary structures among psychrophilic, mesophilic, and thermophilic subtilases revealed that the turn between the β8 and β9 strands (β8-β9 turn, BPN' numbering) of psychrophilic subtilases are more flexible than those of their mesophilic and thermophilic counterparts.
Subtilisin enzymes: Practical protein engineering, 379 (2013)

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