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Overview for MACiE Entry M0167

Version history

General Information

EC Number: 3.4.11.10 (A member of the Hydrolases, Acting on peptide bonds (peptidases), Aminopeptidases)

Enzyme Name: bacterial leucyl aminopeptidase

Biological Species: Aeromonas proteolytica (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • Q01693 - Bacterial leucyl aminopeptidase

Representative PDB Code: 1lok - THE 1.20 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THEAMINOPEPTIDASE FROM AEROMONAS PROTEOLYTICA COMPLEXED WITHTRIS: A TALE OF BUFFER INHIBITION (Resolution = 1.20 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

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Image of protein (n-1)

protein
C00017
CHEBI:36080
water
C00001
CHEBI:15377
amino acid
C00045
CHEBI:59814
protein (n-1)
X00143

Overall Comment: This enzyme releases an N-terminal amino acid preferentially leucine but not glutamic or aspartic acids.


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Stepwise Description of the Reaction

Step 1Glu151 deprotonates the zinc activated water molecule.
Step 2The activated hydroxide attacks the peptide carbonyl in a nucleophilic addition.
Step 3The oxyanion initiates an elimination that cleaves the peptide bond and releases the protein's new N-terminal amino acid, which protonates from Glu151, and the amino acid product.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Glu 151 A Side Chain

Metal Cofactors for M0167

Type Het group Number Chain
zinc ZN 901 A Overview
zinc ZN 902 A Overview

References

  1. W. T. Desmarais et al. (2002), Structure, 10, 1063-1072. The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition.
    Medline: 12176384
  2. G. Chen et al. (1997), Biochemistry, 36, 4278-4286. Mechanistic studies on the aminopeptidase from Aeromonas proteolytica: a two-metal ion mechanism for peptide hydrolysis.
    Medline: 9100023
  3. W. Desmarais et al. (2006), J. Biol. Inorg. Chem., 11, 398-408. The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica.
    Medline: 16596389
  4. C. Stamper et al. (2001), Biochemistry, 40, 7035-7046. Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis.
    Medline: 11401547

Homologue information for M0167 (1lok)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0171 carboxypeptidase A
3.4.17.1
1m4l 3.40.630.10
0.6250.4652Compare

Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ

GOA logo
aminopeptidase activity (molecular function)
extracellular region (cellular component)
proteolysis (biological process)
peptidase activity (molecular function)
hydrolase activity (molecular function)
metal ion binding (molecular function)
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