Aspartate proteases
| Aspartate proteases | ||
|---|---|---|
| Enzyme classification | ||
| EC, category | 3.4.23.- , proteolysis | |
Aspartate proteases (also carboxyl proteases or aspartyl proteases ) are enzymes that can split the peptide bonds of a protein (protein) ( proteolysis ). Aspartate proteases are all endopeptidases .
Reaction mechanism
One molecule of water is consumed per reaction ( hydrolysis ). The water molecule is held in position by the amino acid aspartic acid , which is part of the protease and is also the catalytic center.
Classification according to UniProt / MEROPS
The UniProt Consortium regularly publishes a list of peptidases that categorize these enzymes according to their evolutionary origin. The data in the list are provided with high-quality information and can be called up in the MEROPS database. Closely related molecules are grouped together in families whose identifiers consist of a letter ('A' for aspartate proteases) and a number. Families, in turn, belong to clans whose families are related. Clan identifiers have a letter instead of numbers.
There are 15 aspartate protease families in 7 clans (as of 2009), with clan AA with 6 families being of outstanding importance.
| clan | description | Exemplary enzyme | UniProt | Familys |
|---|---|---|---|---|
| AA | acidic aspartyl proteases (eukaryotes / viruses only); two Asp grouped around H 2 O | Pepsin ( homo sapiens ) | P00790 | A1 A2 A3 A9 A11 A33 |
| FROM | autolytic viral envelope proteins; only one asp involved | Nodavirus peptidase | P12870 | A6 A21 |
| AC | Signal peptidases type II (bacteria only) | Signal peptidase II ( E. coli ) | Q1RGH5 | A8 |
| AD | (two asp) | Presenilin-1 ( Homo sapiens ) | P49768 | A22 A24 |
| AE | (one or two asp) | gpr peptidase ( Bacillus megaterium ) | P22321 | A25 A31 |
| AF | Omptin family; Asp and His bind water | Omptin ( E. coli ) | P09169 | A26 |
| A- | without assignment | A5 |
Important aspartate proteases
- Pepsin (A1)
- Chymosin (Rennin, A1)
- Renin (A1)
- Presenilin (A22)