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PDBsum entry 2taa

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protein metals Protein-protein interface(s) links
Hydrolase (o-glycosyl) PDB id
2taa
Jmol
Contents
Protein chains
478 a.a. *
Metals
_CA ×3
* Residue conservation analysis
PDB id:
2taa
Name: Hydrolase (o-glycosyl)
Title: Structure and possible catalytic residues of taka-amylase a
Structure: Taka-amylase a. Chain: a, b, c. Engineered: yes
Source: Aspergillus oryzae. Organism_taxid: 5062
Biol. unit: Trimer (from PQS)
Resolution:
3.00Å     R-factor:   not given    
Authors: M.Kusunoki,Y.Matsuura,N.Tanaka,M.Kakudo
Key ref: Y.Matsuura et al. (1984). Structure and possible catalytic residues of Taka-amylase A. J Biochem, 95, 697-702. PubMed id: 6609921
Date:
18-Oct-82     Release date:   21-Oct-82    
Supersedes: 1taa
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0C1B3  (AMYA1_ASPOR) -  Alpha-amylase A type-1/2
Seq:
Struc:
499 a.a.
478 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 9 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     cellular_component   7 terms 
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     7 terms  

 

 
J Biochem 95:697-702 (1984)
PubMed id: 6609921  
 
 
Structure and possible catalytic residues of Taka-amylase A.
Y.Matsuura, M.Kusunoki, W.Harada, M.Kakudo.
 
  ABSTRACT  
 
A complete molecular model of Taka-amylase A consisting of 478 amino acid residues was built with the aid of amino acid sequence data. Some typical structural features of the molecule are described. A model fitting of an amylose chain in the catalytic site of the enzyme showed a possible productive binding mode between substrate and enzyme. On the basis of the difference Fourier analysis and the model fitting study, glutamic acid (Glu230) and aspartic acid (Asp297), which are located at the bottom of the cleft, were concluded to be the catalytic residues, serving as the general acid and base, respectively.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21082169 M.Gabriško, and S.Janeček (2011).
Characterization of maltase clusters in the genus Drosophila.
  J Mol Evol, 72, 104-118.  
21234823 S.Bano, S.A.Ul Qader, A.Aman, M.N.Syed, and A.Azhar (2011).
Purification and characterization of novel α-amylase from Bacillus subtilis KIBGE HAS.
  AAPS PharmSciTech, 12, 255-261.  
20552260 E.Hostinová, S.Janecek, and J.Gasperík (2010).
Gene sequence, bioinformatics and enzymatic characterization of alpha-amylase from Saccharomycopsis fibuligera KZ.
  Protein J, 29, 355-364.  
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
21080044 M.Lu, S.Wang, Y.Fang, H.Li, S.Liu, and H.Liu (2010).
Cloning, expression, purification, and characterization of cold-adapted α-amylase from Pseudoalteromonas arctica GS230.
  Protein J, 29, 591-597.  
18552192 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.
  Appl Environ Microbiol, 74, 5168-5177.  
  18997332 K.Yamamoto, H.Miyake, M.Kusunoki, and S.Osaki (2008).
Crystallization and preliminary X-ray analysis of isomaltase from Saccharomyces cerevisiae.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1024-1026.  
17123073 K.Ravi-Kumar, K.S.Venkatesh, and S.Umesh-Kumar (2007).
The 53-kDa proteolytic product of precursor starch-hydrolyzing enzyme of Aspergillus niger has Taka-amylase-like activity.
  Appl Microbiol Biotechnol, 74, 1011-1015.  
18071262 S.Kato, A.Shimizu-Ibuka, K.Mura, A.Takeuchi, C.Tokue, and S.Arai (2007).
Molecular cloning and characterization of an alpha-amylase from Pichia burtonii 15-1.
  Biosci Biotechnol Biochem, 71, 3007-3013.  
  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
16751704 T.Morita, N.Tanaka, A.Hosomi, Y.Giga-Hama, and K.Takegawa (2006).
An alpha-amylase homologue, aah3, encodes a GPI-anchored membrane protein required for cell wall integrity and morphogenesis in Schizosaccharomyces pombe.
  Biosci Biotechnol Biochem, 70, 1454-1463.  
16262690 M.Machovic, B.Svensson, E.A.MacGregor, and S.Janecek (2005).
A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21.
  FEBS J, 272, 5497-5513.  
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.  
15560783 H.Akeboshi, T.Tonozuka, T.Furukawa, K.Ichikawa, H.Aoki, A.Shimonishi, A.Nishikawa, and Y.Sakano (2004).
Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase.
  Eur J Biochem, 271, 4420-4427.  
15291818 K.Yamamoto, A.Nakayama, Y.Yamamoto, and S.Tabata (2004).
Val216 decides the substrate specificity of alpha-glucosidase in Saccharomyces cerevisiae.
  Eur J Biochem, 271, 3414-3420.  
  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.  
12581203 S.Janecek, B.Svensson, and E.A.MacGregor (2003).
Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.
  Eur J Biochem, 270, 635-645.  
11849357 S.P.Kidd, and J.M.Pemberton (2002).
The cloning and characterization of a second alpha-amylase of A. hydrophila JMP636.
  J Appl Microbiol, 92, 289-296.  
11447149 D.J.Smith, W.F.King, L.A.Barnes, D.Trantolo, D.L.Wise, and M.A.Taubman (2001).
Facilitated intranasal induction of mucosal and systemic immunity to mutans streptococcal glucosyltransferase peptide vaccines.
  Infect Immun, 69, 4767-4773.  
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.  
11267650 K.Khajeh, H.Naderi-Manesh, B.Ranjbar, A.Moosavi-Movahedi, and M.Nemat-Gorgani (2001).
Chemical modification of lysine residues in Bacillus alpha-amylases: effect on activity and stability.
  Enzyme Microb Technol, 28, 543-549.  
11302176 T.Yokota, T.Tonozuka, S.Kamitori, and Y.Sakano (2001).
The deletion of amino-terminal domain in Thermoactinomyces vulgaris R-47 alpha-amylases: effects of domain N on activity, specificity, stability and dimerization.
  Biosci Biotechnol Biochem, 65, 401-408.  
11164309 Y.Gueguen, J.L.Rolland, S.Schroeck, D.Flament, S.Defretin, M.H.Saniez, and J.Dietrich (2001).
Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius.
  FEMS Microbiol Lett, 194, 201-206.  
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.  
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.  
10705452 N.Ichikawa, R.Fujisaka, and R.Kuribayashi (2000).
Requirement for lysine-19 of the yeast mitochondrial ATPase inhibitor for the stability of the inactivated inhibitor-F1Fo complex at higher pH.
  Biosci Biotechnol Biochem, 64, 89-95.  
10440673 A.L.Santerre Henriksen, M.Carlsen, H.de Bang, and J.Nielsen (1999).
Kinetics of alpha-amylase secretion in Aspergillus oryzae.
  Biotechnol Bioeng, 65, 76-82.  
10664848 A.Ohnishi, T.Ooi, S.Kinoshita, H.Tomatsuri, K.Umeda, S.Ueda, Y.Hata, and M.Arai (1999).
Analysis of a catalytic acidic pair in the active center of cellulase from Aspergillus aculeatus.
  Biosci Biotechnol Biochem, 63, 2157-2162.  
  10225934 D.J.Smith, R.L.Heschel, W.F.King, and M.A.Taubman (1999).
Antibody to glucosyltransferase induced by synthetic peptides associated with catalytic regions of alpha-amylases.
  Infect Immun, 67, 2638-2642.  
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.  
  9882648 G.P.De Montalk, M.Remaud-Simeon, R.M.Willemot, V.Planchot, and P.Monsan (1999).
Sequence analysis of the gene encoding amylosucrase from Neisseria polysaccharea and characterization of the recombinant enzyme.
  J Bacteriol, 181, 375-381.  
  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.  
  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.  
10430876 R.Kuroki, L.H.Weaver, and B.W.Matthews (1999).
Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site.
  Proc Natl Acad Sci U S A, 96, 8949-8954.
PDB codes: 1qt3 1qt4 1qt5 1qt6 1qt7 1qt8 1qtv 1qtz
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.  
10052123 T.Kobayashi, K.Koike, T.Yoshimatsu, N.Higaki, A.Suzumatsu, T.Ozawa, Y.Hatada, and S.Ito (1999).
Purification and properties of a low-molecular-weight, high-alkaline pectate lyase from an alkaliphilic strain of Bacillus.
  Biosci Biotechnol Biochem, 63, 65-72.  
10089328 T.Yamane, H.Tasaki, F.Matsumoto, A.Suzuki, N.Uozumi, and T.Ashida (1999).
Crystallization and preliminary x-ray analysis of beta-amylase from Bacillus polymyxa.
  Acta Crystallogr D Biol Crystallogr, 55, 898-900.  
9636047 K.Binderup, and J.Preiss (1998).
Glutamate-459 is important for Escherichia coli branching enzyme activity.
  Biochemistry, 37, 9033-9037.  
  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.  
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.  
  9006015 A.R.Reeves, G.R.Wang, and A.A.Salyers (1997).
Characterization of four outer membrane proteins that play a role in utilization of starch by Bacteroides thetaiotaomicron.
  J Bacteriol, 179, 643-649.  
  9293009 G.Dong, C.Vieille, and J.G.Zeikus (1997).
Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme.
  Appl Environ Microbiol, 63, 3577-3584.  
10904554 H.Nakatani (1997).
Monte Carlo simulation of multiple attack mechanism of beta-amylase-catalyzed reaction.
  Biopolymers, 42, 831-836.  
  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.  
9134709 M.F.Grossi de Sa, and M.J.Chrispeels (1997).
Molecular cloning of bruchid (Zabrotes subfasciatus) alpha-amylase cDNA and interactions of the expressed enzyme with bean amylase inhibitors.
  Insect Biochem Mol Biol, 27, 271-281.  
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.  
8611536 C.Braun, T.Lindhorst, N.B.Madsen, and S.G.Withers (1996).
Identification of Asp 549 as the catalytic nucleophile of glycogen-debranching enzyme via trapping of the glycosyl-enzyme intermediate.
  Biochemistry, 35, 5458-5463.  
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.  
8639668 M.R.Sierks, and B.Svensson (1996).
Catalytic mechanism of glucoamylase probed by mutagenesis in conjunction with hydrolysis of alpha-D-glucopyranosyl fluoride and maltooligosaccharides.
  Biochemistry, 35, 1865-1871.  
  8763951 P.Tomme, E.Kwan, N.R.Gilkes, D.G.Kilburn, and R.A.Warren (1996).
Characterization of CenC, an enzyme from Cellulomonas fimi with both endo- and exoglucanase activities.
  J Bacteriol, 178, 4216-4223.  
  8762144 S.Janecek (1996).
Invariant glycines and prolines flanking in loops the strand beta 2 of various (alpha/beta)8-barrel enzymes: a hidden homology?
  Protein Sci, 5, 1136-1143.  
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.  
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.  
  8536970 H.Shibata, and T.Yamazaki (1995).
Molecular evolution of the duplicated Amy locus in the Drosophila melanogaster species subgroup: concerted evolution only in the coding region and an excess of nonsynonymous substitutions in speciation.
  Genetics, 141, 223-236.  
7727505 K.Ara, K.Saeki, K.Igarashi, M.Takaiwa, T.Uemura, H.Hagihara, S.Kawai, and S.Ito (1995).
Purification and characterization of an alkaline amylopullulanase with both alpha-1,4 and alpha-1,6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378.
  Biochim Biophys Acta, 1243, 315-324.  
  7747949 R.D.Wind, W.Liebl, R.M.Buitelaar, D.Penninga, A.Spreinat, L.Dijkhuizen, and H.Bahl (1995).
Cyclodextrin formation by the thermostable alpha-amylase of Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the enzyme as a cyclodextrin glycosyltransferase.
  Appl Environ Microbiol, 61, 1257-1265.  
  7549888 S.Janecek (1995).
Similarity of different beta-strands flanked in loops by glycines and prolines from distinct (alpha/beta)8-barrel enzymes: chance or a homology?
  Protein Sci, 4, 1239-1242.  
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.  
7573841 T.Ohtsuki, Y.Taniguchi, K.Kohno, S.Fukuda, M.Usui, and M.Kurimoto (1995).
Cry j 2, a major allergen of Japanese cedar pollen, shows polymethylgalacturonase activity.
  Allergy, 50, 483-488.  
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.  
  7944355 H.Takata, T.Takaha, T.Kuriki, S.Okada, M.Takagi, and T.Imanaka (1994).
Properties and active center of the thermostable branching enzyme from Bacillus stearothermophilus.
  Appl Environ Microbiol, 60, 3096-3104.  
  8195085 M.Matuschek, G.Burchhardt, K.Sahm, and H.Bahl (1994).
Pullulanase of Thermoanaerobacterium thermosulfurigenes EM1 (Clostridium thermosulfurogenes): molecular analysis of the gene, composite structure of the enzyme, and a common model for its attachment to the cell surface.
  J Bacteriol, 176, 3295-3302.  
  8083158 M.Rimmele, and W.Boos (1994).
Trehalose-6-phosphate hydrolase of Escherichia coli.
  J Bacteriol, 176, 5654-5664.  
  8117096 M.V.Ramesh, S.M.Podkovyrov, S.E.Lowe, and J.G.Zeikus (1994).
Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulanase from Escherichia coli.
  Appl Environ Microbiol, 60, 94.  
  7986049 S.P.Lee, M.Morikawa, M.Takagi, and T.Imanaka (1994).
Cloning of the aapT gene and characterization of its product, alpha-amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601.
  Appl Environ Microbiol, 60, 3764-3773.  
8299155 B.J.Janse, A.J.Steyn, and I.S.Pretorius (1993).
Regional sequence homologies in starch-degrading enzymes.
  Curr Genet, 24, 400-407.  
7505701 G.L.Grossman, and A.A.James (1993).
The salivary glands of the vector mosquito, Aedes aegypti, express a novel member of the amylase gene family.
  Insect Mol Biol, 1, 223-232.  
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.  
  8406882 P.A.Cope, and G.Mooser (1993).
Antibodies against active-site peptides common to glucosyltransferases of mutans streptococci.
  Infect Immun, 61, 4814-4817.  
8141995 S.Janecek, and S.Baláz (1993).
Evolution of parallel beta/alpha-barrel enzyme family lightened by structural data on starch-processing enzymes.
  J Protein Chem, 12, 509-514.  
8099449 T.Keitel, O.Simon, R.Borriss, and U.Heinemann (1993).
Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase.
  Proc Natl Acad Sci U S A, 90, 5287-5291.
PDB codes: 1ayh 1byh
  1400249 A.Geber, P.R.Williamson, J.H.Rex, E.C.Sweeney, and J.E.Bennett (1992).
Cloning and characterization of a Candida albicans maltase gene involved in sucrose utilization.
  J Bacteriol, 174, 6992-6996.  
  1476442 S.Fujiwara, H.Kakihara, K.B.Woo, A.Lejeune, M.Kanemoto, K.Sakaguchi, and T.Imanaka (1992).
Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme.
  Appl Environ Microbiol, 58, 4016-4025.  
  1429471 S.Fujiwara, H.Kakihara, K.Sakaguchi, and T.Imanaka (1992).
Analysis of mutations in cyclodextrin glucanotransferase from Bacillus stearothermophilus which affect cyclization characteristics and thermostability.
  J Bacteriol, 174, 7478-7481.  
1618293 S.Janecek, and S.Baláz (1992).
alpha-Amylases and approaches leading to their enhanced stability.
  FEBS Lett, 304, 1-3.  
  1644767 S.M.Podkovyrov, and J.G.Zeikus (1992).
Structure of the gene encoding cyclomaltodextrinase from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli.
  J Bacteriol, 174, 5400-5405.  
1555585 Y.Suzuki, K.Yonezawa, M.Hattori, and Y.Takii (1992).
Assignment of Bacillus thermoamyloliquefaciens KP1071 alpha-glucosidase I to an exo-alpha-1,4-glucosidase, and its striking similarity to bacillary oligo-1,6-glucosidases in N-terminal sequence and in structural parameters calculated from the amino acid composition.
  Eur J Biochem, 205, 249-256.  
  1938880 E.Rumbak, D.E.Rawlings, G.G.Lindsey, and D.R.Woods (1991).
Characterization of the Butyrivibrio fibrisolvens glgB gene, which encodes a glycogen-branching enzyme with starch-clearing activity.
  J Bacteriol, 173, 6732-6741.  
  2061294 E.Rumbak, D.E.Rawlings, G.G.Lindsey, and D.R.Woods (1991).
Cloning, nucleotide sequence, and enzymatic characterization of an alpha-amylase from the ruminal bacterium Butyrivibrio fibrisolvens H17c.
  J Bacteriol, 173, 4203-4211.  
  1854207 H.Bahl, G.Burchhardt, A.Spreinat, K.Haeckel, A.Wienecke, B.Schmidt, and G.Antranikian (1991).
alpha-Amylase of Clostridium thermosulfurogenes EM1: nucleotide sequence of the gene, processing of the enzyme, and comparison of other alpha-amylases.
  Appl Environ Microbiol, 57, 1554-1559.  
  1917847 T.Kuriki, H.Takata, S.Okada, and T.Imanaka (1991).
Analysis of the active center of Bacillus stearothermophilus neopullulanase.
  J Bacteriol, 173, 6147-6152.  
2340591 D.R.Korman, F.T.Bayliss, C.C.Barnett, C.L.Carmona, K.H.Kodama, T.J.Royer, S.A.Thompson, M.Ward, L.J.Wilson, and R.M.Berka (1990).
Cloning, characterization, and expression of two alpha-amylase genes from Aspergillus niger var. awamori.
  Curr Genet, 17, 203-212.  
2200166 G.K.Farber, and G.A.Petsko (1990).
The evolution of alpha/beta barrel enzymes.
  Trends Biochem Sci, 15, 228-234.  
2150008 H.Bender (1990).
Studies of the mechanism of the cyclisation reaction catalysed by the wildtype and a truncated alpha-cyclodextrin glycosyltransferase from Klebsiella pneumoniae strain M 5 al, and the beta-cyclodextrin glycosyltransferase from Bacillus circulans strain 8.
  Carbohydr Res, 206, 257-267.  
1708883 P.A.Rice, A.Goldman, and T.A.Steitz (1990).
A helix-turn-strand structural motif common in alpha-beta proteins.
  Proteins, 8, 334-340.  
2664768 A.M.Lesk, C.I.Brändén, and C.Chothia (1989).
Structural principles of alpha/beta barrel proteins: the packing of the interior of the sheet.
  Proteins, 5, 139-148.  
  2516722 K.Håkansson, and B.Svensson (1989).
Side chain reactivities of glucoamylase G2 from Aspergillus niger evaluated by group-specific chemical modifications.
  Carlsberg Res Commun, 54, 145-156.  
  2646279 M.Fujita, K.Torigoe, T.Nakada, K.Tsusaki, M.Kubota, S.Sakai, and Y.Tsujisaka (1989).
Cloning and nucleotide sequence of the gene (amyP) for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19.
  J Bacteriol, 171, 1333-1339.  
  2548811 M.Vihinen, and P.Mäntsälä (1989).
Microbial amylolytic enzymes.
  Crit Rev Biochem Mol Biol, 24, 329-418.  
  2464578 N.Uozumi, K.Sakurai, T.Sasaki, S.Takekawa, H.Yamagata, N.Tsukagoshi, and S.Udaka (1989).
A single gene directs synthesis of a precursor protein with beta- and alpha-amylase activities in Bacillus polymyxa.
  J Bacteriol, 171, 375-382.  
2785629 S.Wirsel, A.Lachmund, G.Wildhardt, and E.Ruttkowski (1989).
Three alpha-amylase genes of Aspergillus oryzae exhibit identical intron-exon organization.
  Mol Microbiol, 3, 3.  
3267138 E.A.MacGregor (1988).
Alpha-amylase structure and activity.
  J Protein Chem, 7, 399-415.  
  3257753 H.Satoh, H.Nishida, and K.Isono (1988).
Evidence for movement of the alpha-amylase gene into two phylogenetically distant Bacillus stearothermophilus strains.
  J Bacteriol, 170, 1034-1040.  
  2449422 K.S.Gobius, and J.M.Pemberton (1988).
Molecular cloning, characterization, and nucleotide sequence of an extracellular amylase gene from Aeromonas hydrophila.
  J Bacteriol, 170, 1325-1332.  
  3500166 C.M.Long, M.J.Virolle, S.Y.Chang, S.Chang, and M.J.Bibb (1987).
alpha-Amylase gene of Streptomyces limosus: nucleotide sequence, expression motifs, and amino acid sequence homology to mammalian and invertebrate alpha-amylases.
  J Bacteriol, 169, 5745-5754.  
  3502087 G.Buisson, E.Duée, R.Haser, and F.Payan (1987).
Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity.
  EMBO J, 6, 3909-3916.  
  2957361 K.Kimura, S.Kataoka, Y.Ishii, T.Takano, and K.Yamane (1987).
Nucleotide sequence of the beta-cyclodextrin glucanotransferase gene of alkalophilic Bacillus sp. strain 1011 and similarity of its amino acid sequence to those of alpha-amylases.
  J Bacteriol, 169, 4399-4402.  
  3109866 M.Nishizawa, F.Ozawa, and F.Hishinuma (1987).
Molecular cloning of an amylase gene of Bacillus circulans.
  DNA, 6, 255-265.  
  3029013 S.Hoshiko, O.Makabe, C.Nojiri, K.Katsumata, E.Satoh, and K.Nagaoka (1987).
Molecular cloning and characterization of the Streptomyces hygroscopicus alpha-amylase gene.
  J Bacteriol, 169, 1029-1036.  
3024105 P.H.Boer, and D.A.Hickey (1986).
The alpha-amylase gene in Drosophila melanogaster: nucleotide sequence, gene structure and expression motifs.
  Nucleic Acids Res, 14, 8399-8411.  
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.