CAS 9073-79-4
:Aspartic acid proteinase
Description:
Aspartic acid proteinase, also known as aspartyl protease, is an enzyme that catalyzes the hydrolysis of peptide bonds in proteins, specifically those adjacent to aspartic acid residues. It is characterized by its active site, which contains two aspartate residues that play a crucial role in the catalytic mechanism. This enzyme is typically found in various organisms, including fungi, bacteria, and mammals, and is involved in numerous biological processes, such as protein degradation and processing. Aspartic acid proteinases are known for their role in the digestion of dietary proteins and are also implicated in various physiological and pathological processes, including cell signaling and disease progression. The enzyme operates optimally at acidic pH levels, reflecting its adaptation to environments such as the stomach. Its structure often includes a characteristic fold that stabilizes the active site, allowing for efficient substrate binding and catalysis. Aspartic acid proteinases have applications in biotechnology and pharmaceuticals, particularly in the development of protease inhibitors and therapeutic agents.
Formula:Unspecified
Synonyms:- Aspartic proteinase
- Proteinase, aspartic
- Carboxyl proteinase
- Aspartic acid proteinase
- Aspartyl protease
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Aspartic acid proteinase
CAS:<p>Aspartic acid proteinase is a type of proteolytic enzyme, which originates from various biological sources including humans, fungi, and plants. It is characterized by its action via two critical aspartic acid residues in the active site, which facilitate the hydrolysis of peptide bonds in proteins. This enzyme operates optimally in acidic environments, making it crucial in processes like digestion and protein processing within cellular compartments such as lysosomes.</p>
