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Literature summary for 3.4.11.10 extracted from

  • Schuerer, G.; Lanig, H.; Clark, T.
    Aeromonas proteolytica aminopeptidase: an investigation of the mode of action using a quantum mechanical/molecular mechanical approach (2004), Biochemistry, 43, 5414-5427.
    View publication on PubMed
Search for more literature for 3.4.11.10

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of crystal structures of free Zn-enzyme, and Zn-enyme bound to different inhibitors, complex optimizations, overview Vibrio proteolyticus

Inhibitors

Inhibitors Comment Organism Structure
1-butaneboronic acid binding mode Vibrio proteolyticus
4-iodo-D-phenylalanine hydroxamate binding mode Vibrio proteolyticus
L-leucine phosphonic acid binding mode Vibrio proteolyticus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the metallopeptidase requires two divalent metal ions per enzyme molecule for full activity, binuclear metal center activation and reaction mechanism Vibrio proteolyticus

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus Q01693
-
-

Reaction

Reaction Comment Organism Reaction ID
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. active site structure, reaction mechanism involving divalent metal ions, overview Vibrio proteolyticus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information investigation of the mode of action using a quantum mechanical/molecular mechanical approach Vibrio proteolyticus ?
-
 ?

Synonyms

Synonyms Comment Organism
AAP
-
 Vibrio proteolyticus