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Literature summary for 3.4.11.18 extracted from
- Analysis of the stoichiometric metal activation of methionine aminopeptidase (2009), BMC Biochem., 10, 32.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview | Escherichia coli |  |
| additional information | MetAP belongs to the dinuclear metallohydrolases, mathematical model and detailed analysis of the stoichiometric activation of MetAP by metal cofactors, overview | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MetAP | - |
Escherichia coli |
| methionine aminopeptidase | - |
Escherichia coli |
| More | MetAP belongs to the dinuclear metallohydrolases | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | MetAP is a ubiquitous enzyme required for cell survival and an attractive target for antibacterial and anticancer drug development. MetAP is involved in protein maturation by catalyzing the hydrolytic excision of the N-terminal methionine from nascent proteins | Escherichia coli |
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