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PDBsum entry 1b2y

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protein ligands metals links
Hydrolase PDB id
1b2y
Jmol
Contents
Protein chain
495 a.a. *
Ligands
GLC-G6D-AC1-BGC
PCA
Metals
_CL
_CA
Waters ×105
* Residue conservation analysis
PDB id:
1b2y
Name: Hydrolase
Title: Structure of human pancreatic alpha-amylase in complex with the carbohydrate inhibitor acarbose
Structure: Protein (alpha-amylase). Chain: a. Synonym: hpa. Ec: 3.2.1.1
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: pancreas
Resolution:
3.20Å     R-factor:   0.191     R-free:   0.217
Authors: V.Nahoum,F.Payan
Key ref: V.Nahoum et al. (2000). Crystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitors. Biochem J, 346, 201-208. PubMed id: 10657258
Date:
03-Dec-98     Release date:   16-Feb-00    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04746  (AMYP_HUMAN) -  Pancreatic alpha-amylase
Seq:
Struc:
511 a.a.
495 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.1  - Alpha-amylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   3 terms 
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
Biochem J 346:201-208 (2000)
PubMed id: 10657258  
 
 
Crystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitors.
V.Nahoum, G.Roux, V.Anton, P.Rougé, A.Puigserver, H.Bischoff, B.Henrissat, F.Payan.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20857221 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.
  Mol Biol Rep, 38, 1617-1620.  
20812985 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.
  FEBS J, 277, 4205-4214.
PDB codes: 3a4a 3aj7
20222716 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.
  Biochemistry, 49, 3101-3115.
PDB codes: 3l2l 3l2m
18331662 W.C.Obiro, T.Zhang, and B.Jiang (2008).
The nutraceutical role of the Phaseolus vulgaris alpha-amylase inhibitor.
  Br J Nutr, 100, 1.  
16036768 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.
  Int J Toxicol, 24, 95.  
14511369 N.Oudjeriouat, Y.Moreau, M.Santimone, B.Svensson, G.Marchis-Mouren, and V.Desseaux (2003).
On the mechanism of alpha-amylase.
  Eur J Biochem, 270, 3871-3879.  
12423336 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.
  Eur J Biochem, 269, 5377-5390.  
11856298 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.
  Eur J Biochem, 269, 397-412.  
11257505 E.A.MacGregor, S.Janecek, and B.Svensson (2001).
Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
  Biochim Biophys Acta, 1546, 1.  
11284160 H.J.Gabius (2001).
Glycohistochemistry: the why and how of detection and localization of endogenous lectins.
  Anat Histol Embryol, 30, 3.  
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.