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Literature summary for 3.4.11.10 extracted from

  • Bennett, B.
    EPR of Co(II) as a structural and mechanistic probe of metalloprotein active sites: characterisation of an aminopeptidase (2002), Curr. Top. Biophys., 26, 49-57.
No PubMed abstract available
Search for more literature for 3.4.11.10

Inhibitors

Inhibitors Comment Organism Structure
1-butaneboronic acid binding structure and inhibition mechanism with Co/Zn-, Co/Co-, and Zn/Zn-enzyme Vibrio proteolyticus
L-leucine phosphonic acid transition state inhibitor, binding structure and inhibition mechanism with Co/Zn-, Co/Co-, and Zn/Zn-enzyme Vibrio proteolyticus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Co2+ can substitute for Zn2+ at the the dinuclear active site of the enzyme Vibrio proteolyticus
additional information metalloprotein active site, structure and mechanism overview Vibrio proteolyticus
Zn2+ zinc-dependent metallopeptidase, Co2+ can substitute for Zn2+ at the the dinuclear active site of the enzyme Vibrio proteolyticus

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids active site structure involving His97, Asp117, Asp179, Glu151, Glu152, and His256 Vibrio proteolyticus
a