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PDBsum entry 1lok
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* Residue conservation analysis
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Enzyme class:
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E.C.3.4.11.10
- bacterial leucyl aminopeptidase.
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Reaction:
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
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Cofactor:
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Zn(2+)
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DOI no:
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Structure
10:1063-1072
(2002)
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PubMed id:
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The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition.
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W.T.Desmarais,
D.L.Bienvenue,
K.P.Bzymek,
R.C.Holz,
G.A.Petsko,
D.Ringe.
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ABSTRACT
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The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic
enzyme that removes the N-terminal amino acid from a peptide chain. To fully
understand the metal roles in the reaction pathway of AAP we have solved the
1.20 A resolution crystal structure of native AAP (PDB ID = 1LOK). The
high-quality electron density maps showed a single Tris molecule chelated to the
active site Zn(2+), alternate side chain conformations for some side chains, a
sodium ion that mediates a crystal contact, a surface thiocyanate ion, and
several potential hydrogen atoms. In addition, the high precision of the atomic
positions has led to insight into the protonation states of some of the active
site amino acid side chains.
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Selected figure(s)
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Figure 2.
Figure 2. The Chemical Reaction Mechanism of AAP Based on
Inhibited Structures of AAP and Spectral AnalysisFor clarity,
the metal-coordinating amino acid side chains are only included
in the first step of the reaction mechanism.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
1063-1072)
copyright 2002.
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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.Hartley,
W.Yong,
and
B.Bennett
(2009).
Heterologous expression and purification of Vibrio proteolyticus (Aeromonas proteolytica) aminopeptidase: a rapid protocol.
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Protein Expr Purif,
66,
91.
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PDB code:
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R.Janowski,
T.Auerbach-Nevo,
and
M.S.Weiss
(2008).
Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site.
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Protein Sci,
17,
1138-1150.
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PDB code:
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J.Arima,
Y.Uesugi,
M.Iwabuchi,
and
T.Hatanaka
(2006).
Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica.
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Appl Microbiol Biotechnol,
70,
541-547.
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J.Arima,
Y.Uesugi,
M.Uraji,
M.Iwabuchi,
and
T.Hatanaka
(2006).
Dipeptide synthesis by an aminopeptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides.
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Appl Environ Microbiol,
72,
4225-4231.
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W.Desmarais,
D.L.Bienvenue,
K.P.Bzymek,
G.A.Petsko,
D.Ringe,
and
R.C.Holz
(2006).
The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica.
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J Biol Inorg Chem,
11,
398-408.
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PDB codes:
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K.P.Bzymek,
and
R.C.Holz
(2004).
The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica.
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J Biol Chem,
279,
31018-31025.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
