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 | Methionine aminopeptidase |
Enzyme Information
| 3.4.11.18 |
Methionyl aminopeptidase.
based on mapping to UniProt P0AE18
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
-!- This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. -!- The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val). -!- Belongs to peptidase family M24A.
|
UniProtKB Entries (1)
| P0AE18 |
MAP1_ECOLI
Escherichia coli K-12
Methionine aminopeptidase
|
PDB Structure
| PDB | 1C27 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.
Biochemistry
|
