S7632
N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide
protease substrate
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关于此项目
经验公式（希尔记法）:
C24H34N6O9
化学文摘社编号:
分子量:
550.56
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
产品名称
N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide, protease substrate
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)
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 key
IYHHIHIBYVIDMJ-UHFFFAOYSA-N
assay
≥98% (TLC)
form
powder
solubility
DMF: 10 mg/mL, clear, colorless
UniProt accession no.
storage temp.
−20°C
Quality Level
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)
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
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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
Subtilisin enzymes: Practical protein engineering, 379 (2013)
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.
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