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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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Biochem J
346:201-208
(2000)
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PubMed id:
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Crystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitors.
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V.Nahoum,
G.Roux,
V.Anton,
P.Rougé,
A.Puigserver,
H.Bischoff,
B.Henrissat,
F.Payan.
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ABSTRACT
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Crystal structures of human pancreatic alpha-amylase (HPA) in complex with
naturally occurring inhibitors have been solved. The tetrasaccharide acarbose
and a pseudo-pentasaccharide of the trestatin family produced identical
continuous electron densities corresponding to a pentasaccharide species,
spanning the -3 to +2 subsites of the enzyme, presumably resulting from
transglycosylation. Binding of the acarviosine core linked to a glucose residue
at subsites -1 to +2 appears to be a critical part of the interaction process
between alpha-amylases and trestatin-derived inhibitors. Two crystal forms,
obtained at different values of pH, for the complex of HPA with the protein
inhibitor from Phaseolus vulgaris (alpha-amylase inhibitor) have been solved.
The flexible loop typical of the mammalian alpha-amylases was shown to exist in
two different conformations, suggesting that loop closure is pH-sensitive.
Structural information is provided for the important inhibitor residue, Arg-74,
which has not been observed previously in structural analyses.
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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.Najafian,
A.Ebrahim-Habibi,
N.Hezareh,
P.Yaghmaei,
K.Parivar,
and
B.Larijani
(2011).
Trans-chalcone: a novel small molecule inhibitor of mammalian alpha-amylase.
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Mol Biol Rep, 38,
1617-1620.
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K.Yamamoto,
H.Miyake,
M.Kusunoki,
and
S.Osaki
(2010).
Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose.
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FEBS J, 277,
4205-4214.
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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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W.C.Obiro,
T.Zhang,
and
B.Jiang
(2008).
The nutraceutical role of the Phaseolus vulgaris alpha-amylase inhibitor.
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Br J Nutr, 100,
1.
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K.B.Harikumar,
A.M.Jesil,
M.C.Sabu,
and
R.Kuttan
(2005).
A preliminary assessment of the acute and subchronic toxicity profile of phase2: an alpha-amylase inhibitor.
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Int J Toxicol, 24,
95.
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N.Oudjeriouat,
Y.Moreau,
M.Santimone,
B.Svensson,
G.Marchis-Mouren,
and
V.Desseaux
(2003).
On the mechanism of alpha-amylase.
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Eur J Biochem, 270,
3871-3879.
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H.Mori,
K.S.Bak-Jensen,
and
B.Svensson
(2002).
Barley alpha-amylase Met53 situated at the high-affinity subsite -2 belongs to a substrate binding motif in the beta-->alpha loop 2 of the catalytic (beta/alpha)8-barrel and is critical for activity and substrate specificity.
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Eur J Biochem, 269,
5377-5390.
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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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E.A.MacGregor,
S.Janecek,
and
B.Svensson
(2001).
Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
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Biochim Biophys Acta, 1546,
1.
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H.J.Gabius
(2001).
Glycohistochemistry: the why and how of detection and localization of endogenous lectins.
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Anat Histol Embryol, 30,
3.
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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
