CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.230 | Creatine Amidinohydrolase |
|
3.90.230.10 | Creatinase/methionine aminopeptidase superfamily |
Domain Context
CATH Clusters
| Superfamily | Creatinase/methionine aminopeptidase superfamily |
| Functional Family | Intermediate cleaving peptidase 55 |
Enzyme Information
| 3.4.11.26 |
Intermediate cleaving peptidase 55.
based on mapping to UniProt P40051
The enzyme cleaves the 36-Pro-Pro-37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase.
-!- Icp55 removes the destabilizing N-terminal amino acid residues that are left after cleavage by the mitochondrial processing peptidase, leading to the stabilization of the substrate. -!- The enzyme can remove single amino acids or a short peptide, as in the case of cysteine desulfurase (EC 2.8.1.7), where three amino acids are removed.
|
UniProtKB Entries (1)
| P40051 |
ICP55_YEAST
Saccharomyces cerevisiae S288C
Intermediate cleaving peptidase 55
|
PDB Structure
| PDB | 6A9T |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structures and biochemical analyses of intermediate cleavage peptidase: role of dynamics in enzymatic function.
FEBS Lett.
|