Aspartate protease

Aspartic proteases are a family of eukaryotic protease enzymes that utilize an aspartate residue for catalysis of their peptide substrates. In general, they have two highly-conserved aspartates in the active site and are optimally active at acidic pH. Nearly all known aspartyl proteases are inhibited by pepstatin.

Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. They have a two-domain structure, probably arising from ancestral duplication. Retroviral and retrotransposonproteases (Pfam|PF00077) are much smaller and appear tobe homologous to a single domain of the eukaryotic aspartyl proteases.

Examples

* HIV-1 protease - a major drug-target for treatment of HIV
* Chymosin (or "rennin", with two "n"s)
* Renin (with one "n")
* Cathepsin D
* Pepsin
* Plasmepsin

Mechanism

While a number of different mechanisms for aspartyl proteases have been proposed, the most widely accepted is a general acid-base mechanism involving coordination of a water molecule between the two highly-conserved aspartate residues.cite journal |author=Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR |title=Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue=20 |pages=7009–13 |year=1987 |pmid=3313384 |doi=] cite journal |author=Brik A, Wong CH |title=HIV-1 protease: mechanism and drug discovery |journal=Org. Biomol. Chem. |volume=1 |issue=1 |pages=5–14 |year=2003 |pmid=12929379 |doi=] One aspartate activates the water by abstracting a proton, enabling the water to attack the carbonyl carbon of the substrate scissile bond, generating a tetrahedral oxyanion intermediate. Rearrangement of this intermediate leads to protonation of the scissile amide.

ubfamilies

*Peptidase A1, beta-site APP cleaving enzyme, BACE InterPro|IPR009119

Human proteins containing this domain

BACE; BACE1; BACE2; CTSD; CTSE; NAPSA; PGA5; PGC;
REN;

External links

References

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