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* Residue conservation analysis
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Enzyme class:
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E.C.3.2.1.1
- Alpha-amylase.
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Reaction:
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Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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2 terms
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Biological process
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metabolic process
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3 terms
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Biochemical function
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catalytic activity
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8 terms
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DOI no:
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Biochemistry
40:7700-7709
(2001)
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PubMed id:
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Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex.
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M.Qian,
V.Nahoum,
J.Bonicel,
H.Bischoff,
B.Henrissat,
F.Payan.
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ABSTRACT
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Mammalian alpha-amylases catalyze the hydrolysis of alpha-linked glucose
polymers according to a complex processive mechanism. We have determined the
X-ray structures of porcine pancreatic alpha-amylase complexes with the smallest
molecule of the trestatin family (acarviosine-glucose) which inhibits porcine
pancreatic alpha-amylase and yet is not hydrolyzed by the enzyme. A structure
analysis at 1.38 A resolution of this complex allowed for a clear identification
of a genuine single hexasaccharide species composed of two alpha-1,4-linked
original molecules bound to the active site of the enzyme. The structural
results supported by mass spectrometry experiments provide evidence for an
enzymatically catalyzed condensation reaction in the crystal.
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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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X.Qin,
L.Ren,
X.Yang,
F.Bai,
L.Wang,
P.Geng,
G.Bai,
and
Y.Shen
(2011).
Structures of human pancreatic α-amylase in complex with acarviostatins: Implications for drug design against type II diabetes.
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J Struct Biol, 174,
196-202.
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PDB codes:
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N.M.Koropatkin,
and
T.J.Smith
(2010).
SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules.
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Structure, 18,
200-215.
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PDB codes:
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S.B.Larson,
J.S.Day,
and
A.McPherson
(2010).
X-ray crystallographic analyses of pig pancreatic alpha-amylase with limit dextrin, oligosaccharide, and alpha-cyclodextrin.
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Biochemistry, 49,
3101-3115.
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PDB codes:
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C.Ragunath,
S.G.Manuel,
V.Venkataraman,
H.B.Sait,
C.Kasinathan,
and
N.Ramasubbu
(2008).
Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding.
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J Mol Biol, 384,
1232-1248.
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D.J.Harvey
(2008).
Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update covering the period 2001-2002.
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Mass Spectrom Rev, 27,
125-201.
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J.Y.Damián-Almazo,
A.Moreno,
A.López-Munguía,
X.Soberón,
F.González-Muñoz,
and
G.Saab-Rincón
(2008).
Enhancement of the alcoholytic activity of alpha-amylase AmyA from Thermotoga maritima MSB8 (DSM 3109) by site-directed mutagenesis.
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Appl Environ Microbiol, 74,
5168-5177.
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V.Spiwok,
P.Lipovová,
T.Skálová,
J.Dusková,
J.Dohnálek,
J.Hasek,
N.J.Russell,
and
B.Králová
(2007).
Cold-active enzymes studied by comparative molecular dynamics simulation.
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J Mol Model, 13,
485-497.
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X.Robert,
R.Haser,
H.Mori,
B.Svensson,
and
N.Aghajari
(2005).
Oligosaccharide binding to barley alpha-amylase 1.
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J Biol Chem, 280,
32968-32978.
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PDB codes:
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A.Ohtaki,
M.Mizuno,
T.Tonozuka,
Y.Sakano,
and
S.Kamitori
(2004).
Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.
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J Biol Chem, 279,
31033-31040.
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PDB codes:
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N.Ramasubbu,
C.Ragunath,
P.J.Mishra,
L.M.Thomas,
G.Gyémánt,
and
L.Kandra
(2004).
Human salivary alpha-amylase Trp58 situated at subsite -2 is critical for enzyme activity.
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Eur J Biochem, 271,
2517-2529.
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PDB codes:
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A.Laederach,
and
P.J.Reilly
(2003).
Specific empirical free energy function for automated docking of carbohydrates to proteins.
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J Comput Chem, 24,
1748-1757.
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J.S.Baek,
H.Y.Kim,
T.P.Abbott,
T.W.Moon,
S.B.Lee,
C.S.Park,
and
K.H.Park
(2003).
Acarviosine-simmondsin, a novel compound obtained from acarviosine-glucose and simmondsin by Thermus maltogenic amylase and its in vivo effect on food intake and hyperglycemia.
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Biosci Biotechnol Biochem, 67,
532-539.
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M.Kagawa,
Z.Fujimoto,
M.Momma,
K.Takase,
and
H.Mizuno
(2003).
Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose.
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J Bacteriol, 185,
6981-6984.
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PDB code:
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M.C.Abad,
K.Binderup,
J.Rios-Steiner,
R.K.Arni,
J.Preiss,
and
J.H.Geiger
(2002).
The X-ray crystallographic structure of Escherichia coli branching enzyme.
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J Biol Chem, 277,
42164-42170.
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PDB code:
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N.Aghajari,
G.Feller,
C.Gerday,
and
R.Haser
(2002).
Structural basis of alpha-amylase activation by chloride.
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Protein Sci, 11,
1435-1441.
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PDB codes:
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O.L.Franco,
D.J.Rigden,
F.R.Melo,
and
M.F.Grossi-De-Sá
(2002).
Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.
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Eur J Biochem, 269,
397-412.
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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
codes are
shown on the right.
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Links
