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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1amp

E.C. namebacterial leucyl aminopeptidase
SpeciesVibrio proteolyticus (Aeromonas proteolytica)
E.C. Number (IntEnz) 3.4.11.10
CSA Homologues of 1ampThere are 102 Homologs
CSA Entries With UniProtID Q01693
CSA Entries With EC Number 3.4.11.10
PDBe Entry 1amp
PDBSum Entry 1amp
MACiE Entry M0167

Literature Report

IntroductionAminopeptidases catalyse the hydrolysis of a wide range of N-terminal amino acid residues from proteins and polypeptides. These enzymes have a broad substrate specificity and are widely distributed in bacteria, yeast, plant and animal tissues. Functions of aminopeptidases include protein maturation, protein degradation, hormone level regulation and cell cycle control. Since aminopeptidase activity has been reported on the surface of tumour cells, they are very likely key players in tumour growth and metastatic proliferation.
MechansimA zinc-activated water molecule, deprotonated by glutamate, attacks the carbonyl carbon of the substrate. The tetrahedral oxyanion transition state is stabilised by one of the zinc ions. The transition state collapses, breaking the peptide bond, and the leaving group is protonated by the glutamate residue, returning the enzyme to its native state.

Catalytic Sites for 1amp

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA151257macie:sideChainDeprotonates the nucleophilic water molecule, protonates the leaving group.

Literature References

Notes:
Chen G
Mechanistic studies on the aminopeptidase from Aeromonas proteolytica: a two-metal ion mechanism for peptide hydrolysis.
Biochemistry 1997 36 4278-4286
PubMed: 9100023
Desmarais W
The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica.
J Biol Inorg Chem 2006 11 398-408
PubMed: 16596389
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