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PDBsum entry 1ppi

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protein ligands metals links
Hydrolase (o-glycosyl) PDB id
1ppi
Jmol
Contents
Protein chain
496 a.a. *
Ligands
GLC-GLC-DAF-BGC
Metals
_CA
_CL
Waters ×393
* Residue conservation analysis
PDB id:
1ppi
Name: Hydrolase (o-glycosyl)
Title: The active center of a mammalian alpha-amylase. The structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2 angstroms resolution
Structure: Alpha-amylase. Chain: a. Engineered: yes
Source: Sus scrofa. Pig. Organism_taxid: 9823. Tissue: pancreas
Resolution:
2.20Å     R-factor:   0.153    
Authors: M.Qian,R.Haser,F.Payan
Key ref:
M.Qian et al. (1994). The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution. Biochemistry, 33, 6284-6294. PubMed id: 8193143 DOI: 10.1021/bi00186a031
Date:
22-Feb-94     Release date:   24-May-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00690  (AMYP_PIG) -  Pancreatic alpha-amylase
Seq:
Struc:
511 a.a.
496 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 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   2 terms 
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
DOI no: 10.1021/bi00186a031 Biochemistry 33:6284-6294 (1994)
PubMed id: 8193143  
 
 
The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution.
M.Qian, R.Haser, G.Buisson, E.Duée, F.Payan.
 
  ABSTRACT  
 
An X-ray structure analysis of a crystal of pig pancreatic alpha-amylase (EC 3.2.1.1) that was soaked with acarbose (a pseudotetrasaccharide alpha-amylase inhibitor) showed electron density corresponding to five fully occupied subsites in the active site. The crystal structure was refined to an R-factor of 15.3%, with a root mean square deviation in bond distances of 0.015 A. The model includes all 496 residues of the enzyme, one calcium ion, one chloride ion, 393 water molecules, and five bound sugar rings. The pseudodisaccharide acarviosine that is the essential structural unit responsible for the activity of all inhibitors of the acarbose type was located at the catalytic center. The carboxylic oxygens of the catalytically competent residues Glu233 and Asp300 form hydrogen bonds with the "glycosidic" NH group of the acarviosine group. The third residue of the catalytic triad Asp197 is located on the opposite side of the inhibitor binding cleft with one of its carbonyl oxygens at a 3.3-A distance from the anomeric carbon C-1 of the inhibitor center. Binding of inhibitor induces structural changes at the active site of the enzyme. A loop region between residues 304 and 309 moves in toward the bound saccharide, the resulting maximal mainchain movement being 5 A for His305. The side chain of residue Asp300 rotates upon inhibitor binding and makes strong van der Waals contacts with the imidazole ring of His299. Four histidine residues (His101, His201, His299, and His305) are found to be hydrogen-bonded with the inhibitor. Many protein-inhibitor hydrogen bond interactions are observed in the complex structure, as is clear hydrophobic stacking of aromatic residues with the inhibitor surface. The chloride activator ion and structural calcium ion are hydrogen-bonded via their ligands and water molecules to the catalytic residues.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21397496 S.Park, S.Hyun, and J.Yu (2011).
Selective α-glucosidase substrates and inhibitors containing short aromatic peptidyl moieties.
  Bioorg Med Chem Lett, 21, 2441-2444.  
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
18951544 B.Khemakhem, M.B.Ali, N.Aghajari, M.Juy, R.Haser, and S.Bejar (2009).
Engineering of the alpha-amylase from Geobacillus stearothermophilus US100 for detergent incorporation.
  Biotechnol Bioeng, 102, 380-389.  
19279191 R.Suzuki, Z.Fujimoto, S.Ito, S.Kawahara, S.Kaneko, K.Taira, T.Hasegawa, and A.Kuno (2009).
Crystallographic snapshots of an entire reaction cycle for a retaining xylanase from Streptomyces olivaceoviridis E-86.
  J Biochem, 146, 61-70.
PDB codes: 2d1z 2d20 2d22 2d23 2d24
18951906 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.
  J Mol Biol, 384, 1232-1248.  
18613721 S.Cheluvaraja, M.Mihailescu, and H.Meirovitch (2008).
Entropy and free energy of a mobile protein loop in explicit water.
  J Phys Chem B, 112, 9512-9522.  
18626642 Y.H.Liu, F.P.Lu, Y.Li, J.L.Wang, and C.Gao (2008).
Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations.
  Appl Microbiol Biotechnol, 80, 795-803.  
18157528 Y.H.Liu, F.P.Lu, Y.Li, X.B.Yin, Y.Wang, and C.Gao (2008).
Characterisation of mutagenised acid-resistant alpha-amylase expressed in Bacillus subtilis WB600.
  Appl Microbiol Biotechnol, 78, 85-94.  
18505459 Y.T.Pan, J.D.Carroll, N.Asano, I.Pastuszak, V.K.Edavana, and A.D.Elbein (2008).
Trehalose synthase converts glycogen to trehalose.
  FEBS J, 275, 3408-3420.  
17683331 I.Matsui, and K.Harata (2007).
Implication for buried polar contacts and ion pairs in hyperthermostable enzymes.
  FEBS J, 274, 4012-4022.  
  16511271 S.Z.Fisher, L.Govindasamy, C.Tu, M.Agbandje-McKenna, D.N.Silverman, H.J.Rajaniemi, and R.McKenna (2006).
Structure of human salivary alpha-amylase crystallized in a C-centered monoclinic space group.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 88-93.  
15681870 G.J.Davies, A.M.Brzozowski, Z.Dauter, M.D.Rasmussen, T.V.Borchert, and K.S.Wilson (2005).
Structure of a Bacillus halmapalus family 13 alpha-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 A resolution.
  Acta Crystallogr D Biol Crystallogr, 61, 190-193.
PDB code: 1w9x
16356852 L.Dolecková-Maresová, M.Pavlík, M.Horn, and M.Mares (2005).
De novo design of alpha-amylase inhibitor: a small linear mimetic of macromolecular proteinaceous ligands.
  Chem Biol, 12, 1349-1357.  
16030022 X.Robert, R.Haser, H.Mori, B.Svensson, and N.Aghajari (2005).
Oligosaccharide binding to barley alpha-amylase 1.
  J Biol Chem, 280, 32968-32978.
PDB codes: 1rp8 1rp9 1rpk
15356864 G.André, and V.Tran (2004).
Putative implication of alpha-amylase loop 7 in the mechanism of substrate binding and reaction products release.
  Biopolymers, 75, 95.  
14660599 K.S.Bak-Jensen, G.André, T.E.Gottschalk, G.Paës, V.Tran, and B.Svensson (2004).
Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley alpha-amylase 1.
  J Biol Chem, 279, 10093-10102.  
15182367 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.
  Eur J Biochem, 271, 2517-2529.
PDB codes: 1jxj 1nm9
15304511 S.Numao, I.Damager, C.Li, T.M.Wrodnigg, A.Begum, C.M.Overall, G.D.Brayer, and S.G.Withers (2004).
In situ extension as an approach for identifying novel alpha-amylase inhibitors.
  J Biol Chem, 279, 48282-48291.
PDB codes: 1u2y 1u30 1u33
  16233519 A.Tanaka, and E.Hoshino (2003).
Secondary calcium-binding parameter of Bacillus amyloliquefaciens alpha-amylase obtained from inhibition kinetics.
  J Biosci Bioeng, 96, 262-267.  
12492486 H.Leemhuis, B.W.Dijkstra, and L.Dijkhuizen (2003).
Thermoanaerobacterium thermosulfurigenes cyclodextrin glycosyltransferase.
  Eur J Biochem, 270, 155-162.  
14732931 M.Westerfors, U.Tedebark, H.O.Andersson, S.Ohrman, D.Choudhury, O.Ersoy, Y.Shinohara, A.Axén, E.Carredano, and H.Baumann (2003).
Structure-based discovery of a new affinity ligand to pancreatic alpha-amylase.
  J Mol Recognit, 16, 396-405.  
12511577 S.D'Amico, J.C.Marx, C.Gerday, and G.Feller (2003).
Activity-stability relationships in extremophilic enzymes.
  J Biol Chem, 278, 7891-7896.  
11960990 A.Desmyter, S.Spinelli, F.Payan, M.Lauwereys, L.Wyns, S.Muyldermans, and C.Cambillau (2002).
Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology.
  J Biol Chem, 277, 23645-23650.
PDB codes: 1kxq 1kxt 1kxv
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.  
12021442 N.Aghajari, G.Feller, C.Gerday, and R.Haser (2002).
Structural basis of alpha-amylase activation by chloride.
  Protein Sci, 11, 1435-1441.
PDB codes: 1jd7 1jd9 1l0p
12324460 S.D'Amico, C.Gerday, and G.Feller (2002).
Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase.
  J Biol Chem, 277, 46110-46115.  
12171655 S.D'Amico, P.Claverie, T.Collins, D.Georlette, E.Gratia, A.Hoyoux, M.A.Meuwis, G.Feller, and C.Gerday (2002).
Molecular basis of cold adaptation.
  Philos Trans R Soc Lond B Biol Sci, 357, 917-925.  
11856334 T.P.Frandsen, M.M.Palcic, and B.Svensson (2002).
Substrate recognition by three family 13 yeast alpha-glucosidases.
  Eur J Biochem, 269, 728-734.  
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.  
11737209 H.Mori, K.S.Bak-Jensen, T.E.Gottschalk, M.S.Motawia, I.Damager, B.L.Møller, and B.Svensson (2001).
Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and -5/-6 of barley alpha-amylase 1.
  Eur J Biochem, 268, 6545-6558.  
11288183 J.C.Uitdehaag, B.A.van der Veen, L.Dijkhuizen, R.Elber, and B.W.Dijkstra (2001).
Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase.
  Proteins, 43, 327-335.  
11443082 M.Hemker, A.Stratmann, K.Goeke, W.Schröder, J.Lenz, W.Piepersberg, and H.Pape (2001).
Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50.
  J Bacteriol, 183, 4484-4492.  
11284678 N.Alam, S.Gourinath, S.Dey, A.Srinivasan, and T.P.Singh (2001).
Substrate-inhibitor interactions in the kinetics of alpha-amylase inhibition by ragi alpha-amylase/trypsin inhibitor (RATI) and its various N-terminal fragments.
  Biochemistry, 40, 4229-4233.  
10924103 A.M.Brzozowski, D.M.Lawson, J.P.Turkenburg, H.Bisgaard-Frantzen, A.Svendsen, T.V.Borchert, Z.Dauter, K.S.Wilson, and G.J.Davies (2000).
Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes.
  Biochemistry, 39, 9099-9107.
PDB codes: 1e3x 1e3z 1e40 1e43
10769135 G.D.Brayer, G.Sidhu, R.Maurus, E.H.Rydberg, C.Braun, Y.Wang, N.T.Nguyen, C.M.Overall, and S.G.Withers (2000).
Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques.
  Biochemistry, 39, 4778-4791.
PDB codes: 1cpu 2cpu 3cpu
  11082203 I.Przylas, Y.Terada, K.Fujii, T.Takaha, W.Saenger, and N.Sträter (2000).
X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cyclic glucans.
  Eur J Biochem, 267, 6903-6913.
PDB code: 1esw
11150610 J.E.Nielsen, and T.V.Borchert (2000).
Protein engineering of bacterial alpha-amylases.
  Biochim Biophys Acta, 1543, 253-274.  
11025543 J.Lehtiö, T.T.Teeri, and P.A.Nygren (2000).
Alpha-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold.
  Proteins, 41, 316-322.  
10841756 T.J.Kim, C.S.Park, H.Y.Cho, S.S.Cha, J.S.Kim, S.B.Lee, T.W.Moon, J.W.Kim, B.H.Oh, and K.H.Park (2000).
Role of the glutamate 332 residue in the transglycosylation activity of ThermusMaltogenic amylase.
  Biochemistry, 39, 6773-6780.  
11087936 T.Lonhienne, C.Gerday, and G.Feller (2000).
Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility.
  Biochim Biophys Acta, 1543, 1.  
10866815 V.Monchois, M.Vignon, P.C.Escalier, B.Svensson, and R.R.Russell (2000).
Involvement of Gln937 of Streptococcus downei GTF-I glucansucrase in transition-state stabilization.
  Eur J Biochem, 267, 4127-4136.  
  10198028 C.Brunkhorst, C.Andersen, and E.Schneider (1999).
Acarbose, a pseudooligosaccharide, is transported but not metabolized by the maltose-maltodextrin system of Escherichia coli.
  J Bacteriol, 181, 2612-2619.  
10052953 D.Josse, W.Xie, F.Renault, D.Rochu, L.M.Schopfer, P.Masson, and O.Lockridge (1999).
Identification of residues essential for human paraoxonase (PON1) arylesterase/organophosphatase activities.
  Biochemistry, 38, 2816-2825.  
  10091666 E.H.Rydberg, G.Sidhu, H.C.Vo, J.Hewitt, H.C.Côte, Y.Wang, S.Numao, R.T.MacGillivray, C.M.Overall, G.D.Brayer, and S.G.Withers (1999).
Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris.
  Protein Sci, 8, 635-643.
PDB code: 1bsi
10547530 G.André, A.Buléon, R.Haser, and V.Tran (1999).
Amylose chain behavior in an interacting context. III. Complete occupancy of the AMY2 barley alpha-amylase cleft and comparison with biochemical data.
  Biopolymers, 50, 751-762.  
10872458 H.D.Ly, and S.G.Withers (1999).
Mutagenesis of glycosidases.
  Annu Rev Biochem, 68, 487-522.  
  10473430 J.Abe, C.Ushijima, and S.Hizukuri (1999).
Expression of the isoamylase gene of Flavobacterium odoratum KU in Escherichia coli and identification of essential residues of the enzyme by site-directed mutagenesis.
  Appl Environ Microbiol, 65, 4163-4170.  
10574960 J.C.Uitdehaag, K.H.Kalk, B.A.van Der Veen, L.Dijkhuizen, and B.W.Dijkstra (1999).
The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution.
  J Biol Chem, 274, 34868-34876.
PDB code: 1d3c
10491128 J.E.Nielsen, L.Beier, D.Otzen, T.V.Borchert, H.B.Frantzen, K.V.Andersen, and A.Svendsen (1999).
Electrostatics in the active site of an alpha-amylase.
  Eur J Biochem, 264, 816-824.  
10469642 K.A.Watson, C.McCleverty, S.Geremia, S.Cottaz, H.Driguez, and L.N.Johnson (1999).
Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question.
  EMBO J, 18, 4619-4632.
PDB codes: 1e4o 1qm5
10220320 M.O'Reilly, K.A.Watson, and L.N.Johnson (1999).
The crystal structure of the Escherichia coli maltodextrin phosphorylase-acarbose complex.
  Biochemistry, 38, 5337-5345.
PDB code: 2ecp
10082956 S.Darnis, N.Juge, X.J.Guo, G.Marchis-Mouren, A.Puigserver, and J.C.Chaix (1999).
Molecular cloning and primary structure analysis of porcine pancreatic alpha-amylase.
  Biochim Biophys Acta, 1430, 281-289.  
10089450 V.Nahoum, F.Farisei, V.Le-Berre-Anton, M.P.Egloff, P.Rougé, E.Poerio, and F.Payan (1999).
A plant-seed inhibitor of two classes of alpha-amylases: X-ray analysis of Tenebrio molitor larvae alpha-amylase in complex with the bean Phaseolus vulgaris inhibitor.
  Acta Crystallogr D Biol Crystallogr, 55, 360-362.
PDB code: 1viw
10387084 Z.Dauter, M.Dauter, A.M.Brzozowski, S.Christensen, T.V.Borchert, L.Beier, K.S.Wilson, and G.J.Davies (1999).
X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
  Biochemistry, 38, 8385-8392.
PDB codes: 1qho 1qhp
9755156 G.Parsiegla, M.Juy, C.Reverbel-Leroy, C.Tardif, J.P.Belaïch, H.Driguez, and R.Haser (1998).
The crystal structure of the processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 2.0 A resolution.
  EMBO J, 17, 5551-5562.
PDB code: 1fce
  9726872 K.Igarashi, Y.Hatada, H.Hagihara, K.Saeki, M.Takaiwa, T.Uemura, K.Ara, K.Ozaki, S.Kawai, T.Kobayashi, and S.Ito (1998).
Enzymatic properties of a novel liquefying alpha-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences.
  Appl Environ Microbiol, 64, 3282-3289.  
9551551 M.Machius, N.Declerck, R.Huber, and G.Wiegand (1998).
Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad.
  Structure, 6, 281-292.
PDB code: 1bli
  9541387 N.Aghajari, G.Feller, C.Gerday, and R.Haser (1998).
Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor.
  Protein Sci, 7, 564-572.
PDB codes: 1aqh 1aqm
9862804 N.Aghajari, G.Feller, C.Gerday, and R.Haser (1998).
Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level.
  Structure, 6, 1503-1516.
PDB code: 1b0i
9488711 R.D.Wind, J.C.Uitdehaag, R.M.Buitelaar, B.W.Dijkstra, and L.Dijkhuizen (1998).
Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1.
  J Biol Chem, 273, 5771-5779.
PDB code: 1a47
9860832 R.Mosi, H.Sham, J.C.Uitdehaag, R.Ruiterkamp, B.W.Dijkstra, and S.G.Withers (1998).
Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase.
  Biochemistry, 37, 17192-17198.  
9521706 S.Howard, and S.G.Withers (1998).
Labeling and identification of the postulated acid/base catalyst in the alpha-glucosidase from Saccharomyces cerevisiae using a novel bromoketone C-glycoside.
  Biochemistry, 37, 3858-3864.  
9721603 S.Janecek (1998).
Sequence of archaeal Methanococcus jannaschii alpha-amylase contains features of families 13 and 57 of glycosyl hydrolases: a trace of their common ancestor?
  Folia Microbiol (Praha), 43, 123-128.  
9687373 S.Strobl, K.Maskos, G.Wiegand, R.Huber, F.X.Gomis-Rüth, and R.Glockshuber (1998).
A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution.
  Structure, 6, 911-921.
PDB code: 1tmq
9283074 A.M.Brzozowski, and G.J.Davies (1997).
Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 A resolution.
  Biochemistry, 36, 10837-10845.
PDB code: 7taa
  9293008 G.Dong, C.Vieille, A.Savchenko, and J.G.Zeikus (1997).
Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme.
  Appl Environ Microbiol, 63, 3569-3576.  
9278396 I.Matsui, and B.Svensson (1997).
Improved activity and modulated action pattern obtained by random mutagenesis at the fourth beta-alpha loop involved in substrate binding to the catalytic (beta/alpha)8-barrel domain of barley alpha-amylase 1.
  J Biol Chem, 272, 22456-22463.  
8999834 M.Inohara-Ochiai, T.Nakayama, R.Goto, M.Nakao, T.Ueda, and Y.Shibano (1997).
Altering substrate specificity of Bacillus sp. SAM1606 alpha-glucosidase by comparative site-specific mutagenesis.
  J Biol Chem, 272, 1601-1607.  
9145112 M.O'Reilly, K.A.Watson, R.Schinzel, D.Palm, and L.N.Johnson (1997).
Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase.
  Nat Struct Biol, 4, 405-412.
PDB code: 1ahp
  9385631 M.Qian, S.Spinelli, H.Driguez, and F.Payan (1997).
Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 A resolution.
  Protein Sci, 6, 2285-2296.
PDB code: 1jfh
9245426 R.Mosi, S.He, J.Uitdehaag, B.W.Dijkstra, and S.G.Withers (1997).
Trapping and characterization of the reaction intermediate in cyclodextrin glycosyltransferase by use of activated substrates and a mutant enzyme.
  Biochemistry, 36, 9927-9934.  
9288901 S.Arming, B.Strobl, C.Wechselberger, and G.Kreil (1997).
In vitro mutagenesis of PH-20 hyaluronidase from human sperm.
  Eur J Biochem, 247, 810-814.  
9352636 T.Suganuma, Y.Maeda, K.Kitahara, and T.Nagahama (1997).
Study of the action of human salivary alpha-amylase on 2-chloro-4-nitrophenyl alpha-maltotrioside in the presence of potassium thiocyanate.
  Carbohydr Res, 303, 219-227.  
9019410 Y.P.Yuan, J.Schultz, M.Mlodzik, and P.Bork (1997).
Secreted fringe-like signaling molecules may be glycosyltransferases.
  Cell, 88, 9.  
8805552 A.C.Pike, K.Brew, and K.R.Acharya (1996).
Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase.
  Structure, 4, 691-703.
PDB codes: 1hfx 1hfy 1hfz
8672460 B.Strokopytov, R.M.Knegtel, D.Penninga, H.J.Rozeboom, K.H.Kalk, L.Dijkhuizen, and B.W.Dijkstra (1996).
Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity.
  Biochemistry, 35, 4241-4249.
PDB codes: 1dij 2dij
8994970 C.Bompard-Gilles, P.Rousseau, P.Rougé, and F.Payan (1996).
Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex.
  Structure, 4, 1441-1452.
PDB code: 1dhk
8681972 C.Gilles, J.P.Astier, G.Marchis-Mouren, C.Cambillau, and F.Payan (1996).
Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose.
  Eur J Biochem, 238, 561-569.
PDB code: 1ose
8798613 G.Feller, O.Bussy, C.Houssier, and C.Gerday (1996).
Structural and functional aspects of chloride binding to Alteromonas haloplanctis alpha-amylase.
  J Biol Chem, 271, 23836-23841.  
8879556 J.W.Darrow, and D.G.Drueckhammer (1996).
A cyclic phosphonamidate analogue of glucose as a selective inhibitor of inverting glycosidases.
  Bioorg Med Chem, 4, 1341-1348.  
  8935166 L.A.van den Broek, M.W.Kat-Van Den Nieuwenhof, T.D.Butters, and C.A.Van Boeckel (1996).
Synthesis of alpha-glucosidase I inhibitors showing antiviral (HIV-1) and immunosuppressive activity.
  J Pharm Pharmacol, 48, 172-178.  
8944767 M.Alkazaz, V.Desseaux, G.Marchis-Mouren, F.Payan, E.Forest, and M.Santimone (1996).
The mechanism of porcine pancreatic alpha-amylase. Kinetic evidence for two additional carbohydrate-binding sites.
  Eur J Biochem, 241, 787-796.  
8721743 T.Suganuma, M.Ohnishi, K.Hiromi, and T.Nagahama (1996).
Elucidation of the subsite structure of bacterial saccharifying alpha-amylase and its mode of degradation of maltose.
  Carbohydr Res, 282, 171-180.  
8535789 C.Wiesmann, G.Beste, W.Hengstenberg, and G.E.Schulz (1995).
The three-dimensional structure of 6-phospho-beta-galactosidase from Lactococcus lactis.
  Structure, 3, 961-968.
PDB code: 1pbg
7556163 F.Casset, A.Imberty, R.Haser, F.Payan, and S.Perez (1995).
Molecular modelling of the interaction between the catalytic site of pig pancreatic alpha-amylase and amylose fragments.
  Eur J Biochem, 232, 284-293.  
  8528071 G.D.Brayer, Y.Luo, and S.G.Withers (1995).
The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes.
  Protein Sci, 4, 1730-1742.
PDB code: 1hny
  7613472 M.Qian, R.Haser, and F.Payan (1995).
Carbohydrate binding sites in a pancreatic alpha-amylase-substrate complex, derived from X-ray structure analysis at 2.1 A resolution.
  Protein Sci, 4, 747-755.  
7493956 R.M.Knegtel, B.Strokopytov, D.Penninga, O.G.Faber, H.J.Rozeboom, K.H.Kalk, L.Dijkhuizen, and B.W.Dijkstra (1995).
Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products.
  J Biol Chem, 270, 29256-29264.
PDB codes: 1cxe 1cxf 1cxh 1cxi
7704528 A.C.Terwisscha van Scheltinga, K.H.Kalk, J.J.Beintema, and B.W.Dijkstra (1994).
Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor.
  Structure, 2, 1181-1189.
PDB codes: 1hvm 1hvq
7712292 J.D.McCarter, and S.G.Withers (1994).
Mechanisms of enzymatic glycoside hydrolysis.
  Curr Opin Struct Biol, 4, 885-892.  
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