CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.200 | Peptidase S8/S53 domain |
Domain Context
CATH Clusters
| Superfamily | Peptidase S8/S53 domain |
| Functional Family |
Enzyme Information
| 3.4.21.62 |
Subtilisin.
based on mapping to UniProt P29600
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
-!- Subtilisin is a serine endopeptidase that evolved independently of chymotrypsin. -!- It contains no cysteine residues (although these are found in homologous enzymes). -!- Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase C, nagarse, nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). -!- Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species. -!- Belongs to peptidase family S8. -!- Formerly EC 3.4.4.16 and EC 3.4.21.14.
|
UniProtKB Entries (1)
| P29600 |
SUBS_BACLE
Bacillus lentus
Subtilisin Savinase
|
PDB Structure
| PDB | 1Q5P |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Bacillus |
| Primary Citation |
Do enzymes change the nature of transition states? Mapping the transition state for general acid-base catalysis of a serine protease
Biochemistry
|