Aspartate protease
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| Eukaryotic aspartyl protease | ||
|---|---|---|
| Identifiers | ||
| Symbol | Asp | |
| Pfam | PF00026 | |
| InterPro | IPR001461 | |
| PROSITE | PDOC00128 | |
| SCOP | 1mpp | |
| OPM family | 108 | |
| OPM protein | 1lyb | |
| Available PDB structures:
1j71A:73-383 1eagA:69-386 1zap :69-386 1ypsA:157-477 2rmpA:88-423 2asi :88-423 1mpp :85-420 1bbsA:85-405 1bimB:85-405 1bilA:85-405 1hrnB:85-405 1rne :85-405 1pr7B:85-405 1pr8A:85-405 2ren :85-405 1uhqA:85-405 1g0vA:90-404 1fmxB:90-404 1dp5A:90-404 1fq5A:90-404 1dpjA:90-404 1fq4A:90-404 1fmuA:90-404 2jxrA:90-404 1fq7A:90-404 1fq6A:90-404 1fq8A:90-404 1lywC:78-161 1lybA:78-161 1lyaC:78-161 1b5fB:418-503 1qrpE:75-387 1psn :75-387 1psoE:75-387 1flhA:75-387 3pep :72-384 1f34A:72-384 5pep :72-384 1psaB:72-384 4pep :72-384 3psgA:72-384 1am5 :13-323 1cziE:73-380 1cms :73-380 3cms :73-380 4cms :73-380 1lcgA:77-399 1htrB:72-387 1avfA:72-387 1ls5A:136-446 1miqB:138-448 1qs8B:138-448 1m43B:139-449 1smeA:139-449 1pfzA:139-449 1xe6B:139-449 2bjuA:139-449 1lf3A:139-449 1xdhB:139-449 1leeA:139-449 1xe5A:139-449 2bl3A:139-449 1j8jA:139-449 1me6B:139-449 1lf2A:139-449 1lf4A:139-449 1lduA:138-448 1lcrA:138-448 1qyjA:140-448 1kbxA:138-447 1wkrA:13-332 2er0E:105-419 4er1E:105-419 1epoE:105-419 1oexA:105-419 1entE:105-419 4er4E:105-419 5er1E:105-419 1gvtA:105-419 2er7E:105-419 3er5E:105-419 5er2E:105-419 1oewA:105-419 2er9E:105-419 4er2E:105-419 1e81E:105-419 1gvvA:105-419 1epnE:105-419 3er3E:105-419 4ape :105-419 1epqE:105-419 1gvxA:105-419 1eppE:105-419 1eedP:105-419 1e5oE:105-419 1e82E:105-419 1od1A:105-419 1epmE:105-419 1eprE:105-419 2er6E:105-419 1e80E:105-419 1eplE:105-419 1gvuA:105-419 1er8E:105-419 1gvwA:105-419 1ibqA:84-393 1apvE:16-322 2wec :16-322 2wed :16-322 1ppmE:16-322 1bxoA:16-322 1aptE:16-322 1apwE:16-322 1bxqA:16-322 1pplE:16-322 1apuE:16-322 2web :16-322 1ppkE:16-322 2wea :16-322 3app :16-322 6aprE:84-391 5aprE:84-391 4aprE:84-391 2apr :84-391 3aprE:84-391 1uh8A:83-340 1uh7A:83-340 1uh9A:83-340 1sgzD:74-418 2fdpC:74-418 1xn2B:74-418 2b8vA:74-418 1w51A:74-418 1tqfA:74-418 1xs7D:74-418 1xn3B:74-418 1m4hA:74-418 1ym2A:74-418 1w50A:74-418 2b8lA:74-418 1ym4C:74-418 1fknB:74-418 1yg9A:38-348 |
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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 retrotransposon proteases (Pfam PF00077) are much smaller and appear to be homologous to a single domain of the eukaryotic aspartyl proteases.
Contents |
[edit] 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
[edit] 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.[1][2] 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.
[edit] Subfamilies
- Peptidase A1, beta-site APP cleaving enzyme, BACE IPR009119
[edit] Human proteins containing this domain
BACE; BACE1; BACE2; CTSD; CTSE; NAPSA; PGA5; PGC; REN;
[edit] External links
[edit] References
- ^ a b Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR (1987). "Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action". Proc. Natl. Acad. Sci. U.S.A. 84 (20): 7009–13. PMID 3313384.
- ^ Brik A, Wong CH (2003). "HIV-1 protease: mechanism and drug discovery". Org. Biomol. Chem. 1 (1): 5–14. PMID 12929379.
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