Molecular structure of N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide, CAS Number: 108322-03-8
N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide (CAS 108322-03-8)
Application:
N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide is an enzyme substrate
CAS Number:
108322-03-8
Molecular Weight:
550.56
Molecular Formula:
C24H34N6O9
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.
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SDS & Certificate of Analysis
N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide serves a role in diverse scientific research fields. Its applications encompass the study of protein-protein interactions, protein synthesis, enzyme inhibition, and biochemical assays. This peptide substrate, N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide, facilitates the examination of enzyme activity. By binding to the enzyme′s active site, it triggers the catalytic conversion of the substrate into a product. Subsequently, the product is released, enabling the enzyme to revert to its initial state.
N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide (CAS 108322-03-8) References
- Purification and characterization of an intracellular chymotrypsin-like serine protease from Thermoplasma volcanium. | Kocabiyik, S. and Ozdemir, I. 2006. Biosci Biotechnol Biochem. 70: 126-34. PMID: 16428830
- Substrate specificity and thermostability of the dehairing alkaline protease from Bacillus pumilus. | Wan, MY., et al. 2009. Appl Biochem Biotechnol. 159: 394-403. PMID: 19132554
- A novel isoquinoline alkaloid, DD-carboxypeptidase inhibitor, with antibacterial activity isolated from Streptomyces sp. 8812. Part I: Taxonomy, fermentation, isolation and biological activities. | Solecka, J., et al. 2009. J Antibiot (Tokyo). 62: 575-80. PMID: 19713994
- Gly or Ala substitutions for Pro(210)Thr(211)Asn(212) at the β8-β9 turn of subtilisin Carlsberg increase the catalytic rate and decrease thermostability. | Fuchita, N., et al. 2012. Biochim Biophys Acta. 1824: 620-6. PMID: 22326746
- Structural and mechanistic insights into collagen degradation by a bacterial collagenolytic serine protease in the subtilisin family. | Ran, LY., et al. 2013. Mol Microbiol. 90: 997-1010. PMID: 24112706
- Calcium-induced Tetramerization and Zinc Chelation Shield Human Calprotectin from Degradation by Host and Bacterial Extracellular Proteases. | Stephan, JR. and Nolan, EM. 2016. Chem Sci. 7: 1962-1975. PMID: 26925211
- Characterization of a New S8 serine Protease from Marine Sedimentary Photobacterium sp. A5-7 and the Function of Its Protease-Associated Domain. | Li, HJ., et al. 2016. Front Microbiol. 7: 2016. PMID: 28066343
- Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, at 1.4 Å resolution: Structural adaptations to cold and functional analysis of a laundry detergent enzyme. | Park, HJ., et al. 2018. PLoS One. 13: e0191740. PMID: 29466378
- Marine microbial alkaline protease: An efficient and essential tool for various industrial applications. | Barzkar, N. 2020. Int J Biol Macromol. 161: 1216-1229. PMID: 32534091
Substrate of:
Enzyme.Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
N-Succinyl-Ala-Ala-Val-Ala p-nitroanilide, 25 mg | sc-215479 | 25 mg | $151.00 |