 |
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.3.4.11.2
- Membrane alanyl aminopeptidase.
|
|
|
|
|
|
|
Reaction:
|
|
Release of an N-terminal amino acid, Xaa-|-Xbb- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
|
|
|
|
|
|
Cofactor:
|
|
Zinc
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Biological process
|
proteolysis
|
1 term
|
|
|
Biochemical function
|
hydrolase activity
|
5 terms
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Proteins
70:273-279
(2008)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis.
|
|
B.Nocek,
R.Mulligan,
M.Bargassa,
F.Collart,
A.Joachimiak.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
|
|
Figure 1.
Figure 1. Ribbon presentation of the overall fold of
aminopeptidase N from N. meningitidis showing domain
organization. The N-terminal domain (domain I) is colored
yellow, the catalytic domain (domain II) is colored red, domain
III is colored blue, the C-terminal (domain IV) is colored
green. Each of the domains is also displayed side by side with
the schematic representation of the domain's topology.
|
|
Figure 2.
Figure 2. (A) Close-up view showing the relative positioning of
the bestatin molecule (orange) in the active site of APN-Nm
based on superimposition of the structure of human leukotriene
A[4] hydrolase (1hs6) (teal) over the structure of APN-Nm (red)
using SSM server.[20] (B) Close-up view showing the active site
environment of APN-Nm (domain II).
|
|
|
|
|
|
| |
The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
70,
273-279)
copyright 2008.
|
|
| |
Figures were
selected
by an automated process.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
J.Su,
Q.Wang,
J.Feng,
C.Zhang,
D.Zhu,
T.Wei,
W.Xu,
and
L.Gu
(2011).
Engineered Thermoplasma acidophilum factor F3 mimics human aminopeptidase N (APN) as a target for anticancer drug development.
|
| |
Bioorg Med Chem, 19,
2991-2996.
|
|
|
|
|
|
|
B.P.Nocek,
D.M.Gillner,
Y.Fan,
R.C.Holz,
and
A.Joachimiak
(2010).
Structural basis for catalysis by the mono- and dimetalated forms of the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase.
|
| |
J Mol Biol, 397,
617-626.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
S.Vaiyapuri,
S.C.Wagstaff,
K.A.Watson,
R.A.Harrison,
J.M.Gibbins,
and
E.G.Hutchinson
(2010).
Purification and functional characterisation of rhiminopeptidase A, a novel aminopeptidase from the venom of Bitis gabonica rhinoceros.
|
| |
PLoS Negl Trop Dis, 4,
e796.
|
|
|
|
|
|
|
M.C.Fournié-Zaluski,
H.Poras,
B.P.Roques,
Y.Nakajima,
K.Ito,
and
T.Yoshimoto
(2009).
Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250.
|
| |
Acta Crystallogr D Biol Crystallogr, 65,
814-822.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
M.Grabowski,
M.Chruszcz,
M.D.Zimmerman,
O.Kirillova,
and
W.Minor
(2009).
Benefits of structural genomics for drug discovery research.
|
| |
Infect Disord Drug Targets, 9,
459-474.
|
|
|
|
|
|
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
codes are
shown on the right.
|
|
Links
