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PDBsum entry 2aaa

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protein metals links
Glycosidase PDB id
2aaa
Jmol
Contents
Protein chain
476 a.a. *
Metals
_CA ×2
Waters ×350
* Residue conservation analysis
PDB id:
2aaa
Name: Glycosidase
Title: Calcium binding in alpha-amylases: an x-ray diffraction stud angstroms resolution of two enzymes from aspergillus
Structure: Alpha-amylase. Chain: a. Engineered: yes
Source: Aspergillus niger. Organism_taxid: 5061
Biol. unit: Dimer (from PQS)
Resolution:
2.12Å     R-factor:   0.169    
Authors: L.Brady,A.M.Brzozowski,Z.Derewenda,E.J.Dodson,G.G.Dodson
Key ref:
E.Boel et al. (1990). Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus. Biochemistry, 29, 6244-6249. PubMed id: 2207069 DOI: 10.1021/bi00478a019
Date:
27-Feb-91     Release date:   15-Jul-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P56271  (AMYA_ASPNG) -  Acid alpha-amylase
Seq:
Struc:
484 a.a.
476 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!
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     7 terms  

 

 
DOI no: 10.1021/bi00478a019 Biochemistry 29:6244-6249 (1990)
PubMed id: 2207069  
 
 
Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus.
E.Boel, L.Brady, A.M.Brzozowski, Z.Derewenda, G.G.Dodson, V.J.Jensen, S.B.Petersen, H.Swift, L.Thim, H.F.Woldike.
 
  ABSTRACT  
 
X-ray diffraction analysis (at 2.1-A resolution) of an acid alpha-amylase from Aspergillus niger allowed a detailed description of the stereochemistry of the calcium-binding sites. The primary site (which is essential in maintaining proper folding around the active site) contains a tightly bound Ca2+ with an unusually high number of eight ligands (O delta 1 and O delta 2 of Asp175, O delta of Asn121, main-chain carbonyl oxygens of Glu162 and Glu210, and three water molecules). A secondary binding site was identified at the bottom of the substrate binding cleft; it involves the residues presumed to play a catalytic role (Asp206 and Glu230). This explains the inhibitory effect of calcium observed at higher concentrations. Neutral Aspergillus oryzae (TAKA) alpha-amylase was also refined in a new crystal at 2.1-A resolution. The structure of this homologous (over 80%) enzyme and additional kinetic studies support all the structural conclusions regarding both calcium-binding sites.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20722697 A.Vinck, C.de Bekker, A.Ossin, R.A.Ohm, R.P.de Vries, and H.A.Wösten (2011).
Heterogenic expression of genes encoding secreted proteins at the periphery of Aspergillus niger colonies.
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21426903 L.C.Tsai, C.H.Hsiao, W.Y.Liu, L.M.Yin, and L.F.Shyur (2011).
Structural basis for the inhibition of 1,3-1,4-β-d-glucanase by noncompetitive calcium ion and competitive Tris inhibitors.
  Biochem Biophys Res Commun, 407, 593-598.  
21365786 M.C.Santa-Maria, C.G.Yencho, C.H.Haigler, W.F.Thompson, R.M.Kelly, and B.Sosinski (2011).
Starch self-processing in transgenic sweet potato roots expressing a hyperthermophilic α-amylase.
  Biotechnol Prog, 27, 351-359.  
21111049 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.
  J Struct Biol, 174, 196-202.
PDB codes: 3old 3ole 3olg 3oli
19834705 K.M.Park, S.Y.Jun, K.H.Choi, K.H.Park, C.S.Park, and J.Cha (2010).
Characterization of an exo-acting intracellular alpha-amylase from the hyperthermophilic bacterium Thermotoga neapolitana.
  Appl Microbiol Biotechnol, 86, 555-566.  
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
19763902 O.Prakash, and N.Jaiswal (2010).
alpha-Amylase: an ideal representative of thermostable enzymes.
  Appl Biochem Biotechnol, 160, 2401-2414.  
19585523 M.C.Santa-Maria, C.J.Chou, G.C.Yencho, C.H.Haigler, W.F.Thompson, R.M.Kelly, and B.Sosinski (2009).
Plant cell calcium-rich environment enhances thermostability of recombinantly produced alpha-amylase from the hyperthermophilic bacterium Thermotoga maritime.
  Biotechnol Bioeng, 104, 947-956.  
18320228 X.L.Yuan, R.M.van der Kaaij, C.A.van den Hondel, P.J.Punt, M.J.van der Maarel, L.Dijkhuizen, and A.F.Ram (2008).
Aspergillus niger genome-wide analysis reveals a large number of novel alpha-glucan acting enzymes with unexpected expression profiles.
  Mol Genet Genomics, 279, 545-561.  
18473149 Y.Xu, M.Yang, J.Sun, J.Qian, D.Zhang, Y.Sun, L.Ma, and C.Zhu (2008).
Glycogen branching enzyme: a novel deltamethrin resistance-associated gene from Culex pipiens pallens.
  Parasitol Res, 103, 449-458.  
17496125 R.M.van der Kaaij, X.L.Yuan, A.Franken, A.F.Ram, P.J.Punt, M.J.van der Maarel, and L.Dijkhuizen (2007).
Two novel, putatively cell wall-associated and glycosylphosphatidylinositol-anchored alpha-glucanotransferase enzymes of Aspergillus niger.
  Eukaryot Cell, 6, 1178-1188.  
17597061 S.Ravaud, X.Robert, H.Watzlawick, R.Haser, R.Mattes, and N.Aghajari (2007).
Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization.
  J Biol Chem, 282, 28126-28136.
PDB codes: 1zja 2pwd 2pwe 2pwf 2pwg 2pwh
18086434 T.Suganuma, K.Fujita, and K.Kitahara (2007).
Some distinguishable properties between acid-stable and neutral types of alpha-amylases from acid-producing koji.
  J Biosci Bioeng, 104, 353-362.  
  16880540 A.Vujicić-Zagar, and B.W.Dijkstra (2006).
Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 angstroms resolution.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 716-721.
PDB codes: 2guy 2gvy
16703471 L.L.Lin, P.J.Chen, J.S.Liu, W.C.Wang, and H.F.Lo (2006).
Identification of glutamate residues important for catalytic activity or thermostability of a truncated Bacillus sp. strain TS-23 alpha-amylase by site-directed mutagenesis.
  Protein J, 25, 232-239.  
17068753 N.Wang, Y.Zhang, Q.Wang, J.Liu, H.Wang, Y.Xue, and Y.Ma (2006).
Gene cloning and characterization of a novel alpha-amylase from alkaliphilic Alkalimonas amylolytica.
  Biotechnol J, 1, 1258-1265.  
15722449 R.Maurus, A.Begum, H.H.Kuo, A.Racaza, S.Numao, C.Andersen, J.W.Tams, J.Vind, C.M.Overall, S.G.Withers, and G.D.Brayer (2005).
Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase.
  Protein Sci, 14, 743-755.
PDB codes: 1xgz 1xh0 1xh1 1xh2
14760745 A.Linden, and M.Wilmanns (2004).
Adaptation of class-13 alpha-amylases to diverse living conditions.
  Chembiochem, 5, 231-239.  
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.  
12482867 A.Linden, O.Mayans, W.Meyer-Klaucke, G.Antranikian, and M.Wilmanns (2003).
Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc.
  J Biol Chem, 278, 9875-9884.
PDB codes: 1mwo 1mxd 1mxg
  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.  
12752453 H.B.Fritzsche, T.Schwede, and G.E.Schulz (2003).
Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92.
  Eur J Biochem, 270, 2332-2341.
PDB code: 1h3g
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.  
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.  
12719434 T.Nonaka, M.Fujihashi, A.Kita, H.Hagihara, K.Ozaki, S.Ito, and K.Miki (2003).
Crystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) and its sodium ion binding sites.
  J Biol Chem, 278, 24818-24824.
PDB codes: 1ud2 1ud3 1ud4 1ud5 1ud6 1ud8
12906828 X.Robert, R.Haser, T.E.Gottschalk, F.Ratajczak, H.Driguez, B.Svensson, and N.Aghajari (2003).
The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs.
  Structure, 11, 973-984.
PDB codes: 1ht6 1p6w
12196524 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.
  J Biol Chem, 277, 42164-42170.
PDB code: 1m7x
12214313 P.Constans (2002).
Linear scaling approaches to quantum macromolecular similarity: evaluating the similarity function.
  J Comput Chem, 23, 1305-1313.  
11238984 C.Vieille, and G.J.Zeikus (2001).
Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
  Microbiol Mol Biol Rev, 65, 1.  
11898335 J.W.Kim, H.A.Terc, L.O.Flowers, M.Whiteley, and T.L.Peeples (2001).
Novel, thermostable family-13-like glycoside hydrolase from Methanococcus jannaschii.
  Folia Microbiol (Praha), 46, 475-481.  
11898334 J.W.Kim, L.O.Flowers, M.Whiteley, and T.L.Peeples (2001).
Biochemical confirmation and characterization of the family-57-like alpha-amylase of Methanococcus jannaschii.
  Folia Microbiol (Praha), 46, 467-473.  
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
10689077 D.A.MacKenzie, D.J.Jeenes, X.Gou, and D.B.Archer (2000).
Molecular basis of glucoamylase overproduction by a mutagenised industrial strain of Aspergillus niger.
  Enzyme Microb Technol, 26, 193-200.  
10869188 D.J.Nichols, P.L.Keeling, M.Spalding, and H.Guan (2000).
Involvement of conserved aspartate and glutamate residues in the catalysis and substrate binding of maize starch synthase.
  Biochemistry, 39, 7820-7825.  
11150610 J.E.Nielsen, and T.V.Borchert (2000).
Protein engineering of bacterial alpha-amylases.
  Biochim Biophys Acta, 1543, 253-274.  
10877806 K.Ohdan, T.Kuriki, H.Takata, H.Kaneko, and S.Okada (2000).
Introduction of raw starch-binding domains into Bacillus subtilis alpha-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase.
  Appl Environ Microbiol, 66, 3058-3064.  
10792537 L.Janda, J.Damborský, M.Petrícek, J.Spízek, and P.Tichý (2000).
Molecular characterization of the Thermomonospora curvata aglA gene encoding a thermotolerant alpha-1,4-glucosidase.
  J Appl Microbiol, 88, 773-783.  
9894008 F.Lipari, and A.Herscovics (1999).
Calcium binding to the class I alpha-1,2-mannosidase from Saccharomyces cerevisiae occurs outside the EF hand motif.
  Biochemistry, 38, 1111-1118.  
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.  
10194383 G.Feller, D.d'Amico, and C.Gerday (1999).
Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis.
  Biochemistry, 38, 4613-4619.  
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.  
  10508102 K.Ohdan, T.Kuriki, H.Kaneko, J.Shimada, T.Takada, Z.Fujimoto, H.Mizuno, and S.Okada (1999).
Characteristics of two forms of alpha-amylases and structural implication.
  Appl Environ Microbiol, 65, 4652-4658.  
10099546 L.M.Marchal, J.Jonkers, G.T.Franke, C.D.de Gooijer, and J.Tramper (1999).
The effect of process conditions on the alpha-amylolytic hydrolysis of amylopectin potato starch: An experimental design approach.
  Biotechnol Bioeng, 62, 348-357.  
10350455 S.J.Charnock, and G.J.Davies (1999).
Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms.
  Biochemistry, 38, 6380-6385.
PDB codes: 1qg8 1qgq 1qgs
10586502 S.Kashiwabara, S.Ogawa, N.Miyoshi, M.Oda, and Y.Suzuki (1999).
Three domains comprised in thermostable molecular weight 54,000 pullulanase of type I from Bacillus flavocaldarius KP1228.
  Biosci Biotechnol Biochem, 63, 1736-1748.  
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
9558324 A.K.Schmidt, S.Cottaz, H.Driguez, and G.E.Schulz (1998).
Structure of cyclodextrin glycosyltransferase complexed with a derivative of its main product beta-cyclodextrin.
  Biochemistry, 37, 5909-5915.
PDB code: 3cgt
9730830 B.Z.Yu, J.Rogers, G.R.Nicol, K.H.Theopold, K.Seshadri, S.Vishweshwara, and M.K.Jain (1998).
Catalytic significance of the specificity of divalent cations as KS* and kcat* cofactors for secreted phospholipase A2.
  Biochemistry, 37, 12576-12587.  
9636047 K.Binderup, and J.Preiss (1998).
Glutamate-459 is important for Escherichia coli branching enzyme activity.
  Biochemistry, 37, 9033-9037.  
9853672 K.Funane, N.Libessart, D.Stewart, T.Michishita, and J.Preiss (1998).
Analysis of essential histidine residues of maize branching enzymes by chemical modification and site-directed mutagenesis.
  J Protein Chem, 17, 579-590.  
9805372 K.Ikawa, H.Araki, Y.Tsujino, Y.Hayashi, K.Igarashi, Y.Hatada, H.Hagihara, T.Ozawa, K.Ozaki, T.Kobayashi, and S.Ito (1998).
Hyperexpression of the gene for a Bacillus alpha-amylase in Bacillus subtilis cells: enzymatic properties and crystallization of the recombinant enzyme.
  Biosci Biotechnol Biochem, 62, 1720-1725.  
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
  9385633 A.C.Wallace, N.Borkakoti, and J.M.Thornton (1997).
TESS: a geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites.
  Protein Sci, 6, 2308-2323.  
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.  
  9416598 K.S.Devulapalle, S.D.Goodman, Q.Gao, A.Hemsley, and G.Mooser (1997).
Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutans streptococci.
  Protein Sci, 6, 2489-2493.  
18576090 M.E.Himmel, P.A.Karplus, J.Sakon, W.S.Adney, J.O.Baker, and S.R.Thomas (1997).
Polysaccharide hydrolase folds diversity of structure and convergence of function.
  Appl Biochem Biotechnol, 63, 315-325.  
9360973 T.Kuriki, D.C.Stewart, and J.Preiss (1997).
Construction of chimeric enzymes out of maize endosperm branching enzymes I and II: activity and properties.
  J Biol Chem, 272, 28999-29004.  
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.  
  9006052 W.Liebl, I.Stemplinger, and P.Ruile (1997).
Properties and gene structure of the Thermotoga maritima alpha-amylase AmyA, a putative lipoprotein of a hyperthermophilic bacterium.
  J Bacteriol, 179, 941-948.  
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.  
8605217 K.Maruta, K.Hattori, T.Nakada, M.Kubota, T.Sugimoto, and M.Kurimoto (1996).
Cloning and sequencing of trehalose biosynthesis genes from Arthrobacter sp. Q36.
  Biochim Biophys Acta, 1289, 10-13.  
8916916 M.J.Kahn, T.Kieber-Emmons, G.Vilaire, R.Murali, M.Poncz, and J.S.Bennett (1996).
Effect of mutagenesis of GPIIb amino acid 273 on the expression and conformation of the platelet integrin GPIIb-IIIa.
  Biochemistry, 35, 14304-14311.  
8804578 T.Kuriki, H.Guan, M.Sivak, and J.Preiss (1996).
Analysis of the active center of branching enzyme II from maize endosperm.
  J Protein Chem, 15, 305-313.  
8663322 T.Kuriki, H.Kaneko, M.Yanase, H.Takata, J.Shimada, S.Handa, T.Takada, H.Umeyama, and S.Okada (1996).
Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center.
  J Biol Chem, 271, 17321-17329.  
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.  
  7607219 B.Conrad, V.Hoang, A.Polley, and J.Hofemeister (1995).
Hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylases. Construction, properties and sequence determinants.
  Eur J Biochem, 230, 481-490.  
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
8535779 G.Davies, and B.Henrissat (1995).
Structures and mechanisms of glycosyl hydrolases.
  Structure, 3, 853-859.  
8749857 S.Knapp, A.Rüdiger, G.Antranikian, P.L.Jorgensen, and R.Ladenstein (1995).
Crystallization and preliminary crystallographic analysis of an amylopullulanase from the hyperthermophilic archaeon Pyrococcus woesei.
  Proteins, 23, 595-597.  
8125253 A.P.Kelly, B.Diderichsen, S.Jorgensen, and D.J.McConnell (1994).
Molecular genetic analysis of the pullulanase B gene of Bacillus acidopullulyticus.
  FEMS Microbiol Lett, 115, 97.  
8174545 A.Totsuka, V.H.Nong, H.Kadokawa, C.S.Kim, Y.Itoh, and C.Fukazawa (1994).
Residues essential for catalytic activity of soybean beta-amylase.
  Eur J Biochem, 221, 649-654.  
7813489 B.Schwermann, K.Pfau, B.Liliensiek, M.Schleyer, T.Fischer, and E.P.Bakker (1994).
Purification, properties and structural aspects of a thermoacidophilic alpha-amylase from Alicyclobacillus acidocaldarius atcc 27009. Insight into acidostability of proteins.
  Eur J Biochem, 226, 981-991.  
7881905 G.E.Norris, T.J.Stillman, B.F.Anderson, and E.N.Baker (1994).
The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum.
  Structure, 2, 1049-1059.
PDB code: 1pgs
8168517 K.W.Rodenburg, N.Juge, X.J.Guo, M.Søgaard, J.C.Chaix, and B.Svensson (1994).
Domain B protruding at the third beta strand of the alpha/beta barrel in barley alpha-amylase confers distinct isozyme-specific properties.
  Eur J Biochem, 221, 277-284.  
8200344 T.Keitel, M.Meldgaard, and U.Heinemann (1994).
Cation binding to a Bacillus (1,3-1,4)-beta-glucanase. Geometry, affinity and effect on protein stability.
  Eur J Biochem, 222, 203-214.
PDB code: 1glh
8319688 A.Totsuka, and C.Fukazawa (1993).
Expression and mutation of soybean beta-amylase in Escherichia coli.
  Eur J Biochem, 214, 787-794.  
8136030 H.M.Jespersen, E.A.MacGregor, B.Henrissat, M.R.Sierks, and B.Svensson (1993).
Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes.
  J Protein Chem, 12, 791-805.  
8143291 T.S.Black, L.Kiss, D.Tull, and S.G.Withers (1993).
N-bromoacetyl-glycopyranosylamines as affinity labels for a beta-glucosidase and a cellulase.
  Carbohydr Res, 250, 195-202.  
1730228 M.P.Brosnan, C.T.Kelly, and W.M.Fogarty (1992).
Investigation of the mechanisms of irreversible thermoinactivation of Bacillus stearothermophilus alpha-amylase.
  Eur J Biochem, 203, 225-231.  
1618293 S.Janecek, and S.Baláz (1992).
alpha-Amylases and approaches leading to their enhanced stability.
  FEBS Lett, 304, 1-3.  
1367675 A.Fontana (1991).
Analysis and modulation of protein stability.
  Curr Opin Biotechnol, 2, 551-560.  
1749776 N.Ramasubbu, K.K.Bhandary, F.A.Scannapieco, and M.J.Levine (1991).
Crystallization and preliminary X-ray diffraction studies of human salivary alpha-amylase.
  Proteins, 11, 230-232.  
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