このページはRCSBの David S. Goodsell博士による「Molecule of the Month」2006年2月の記事を日本語に訳したものです。転載・引用については利用規約をご覧下さい。
「今月の分子」一覧に戻る / この記事のRCSBオリジナルサイト(英語)を見る
:翻訳 工藤高裕 (PDBj)
α-アミラーゼ(PDB:1ppi) 中央にある黄色の分子は基質の糖

グルコース(glucose、ぶどう糖)は体内の主要なエネルギー源であるが、残念ながら遊離状態のグルコースは食事の中にあまり含まれていない。その代わり、グルコースはより大きな形で見つかる。それには2つの小さな糖がつながったラクトース(lactose、乳糖)やしょ糖(sucrose、蔗糖)、そしてグルコースが鎖状に長く連なったでんぷん(starch、澱粉)やグリコーゲン(glycogen)が含まれる。消化における主な仕事の1つはこれらの鎖を個々のグルコース単位へと分解することであり、分解されたグルコースは血液によって身体全体の空腹な細胞へと運ばれる。

でんぷんへの攻撃

α-アミラーゼ(alpha-amylase)はでんぷんの分解を開始する。でんぷんの鎖を取り込んで、2、3個のグルコース単位でできた断片へと分解する。2種類の似たアミラーゼが体内で作られている。1つは唾液(saliva)に分泌されるもので、噛むことによりでんぷん粒子の分解が開始される。もう1つはすい臓(pancrea、膵臓)によって分泌されるもので、こちらが仕事を完了させる。そして、腸の壁につなぎ止められた一連の酵素によって個々のグルコース単位へと細かく分解される。

反応中のアミラーゼ

アミラーゼは腸内の気持ちよくない環境で仕事を行う必要があるため、その好ましくない条件に耐えるよう小さくて安定な酵素となっている。ここに示したアミラーゼ(PDBエントリー 1ppi )はブタのすい臓から得られたものである。5つの糖単位でできた小さな鎖(黄色)が、酵素の大きな割れ目に見られる活性部位に結合している。2種類のヒト由来の酵素(ブタのものと非常によく似ている)の構造も、PDBエントリー 1smd1hny で見ることができる。PDBデータベースを見ると、他にも細菌や植物由来のα-アミラーゼおよびでんぷん消化酵素の構造をたくさん見つけることができる。

なお、遺伝的視点から見た追加情報が、欧州バイオインフォマティクス研究所(EBI)の「 今月のタンパク質 」で提供されているので合わせて参照いただきたい。

工業の力

左:コウジカビのアミラーゼ(PDB:2taa) 中央:グルコアミラーゼ(PDB:1dog) 右:グルコース異性化酵素(PDB:4xia)

α-アミラーゼは高果糖コーンシロップ(high fructose corn syrup、HFCS) の生産において大量に使われる。これはトウモロコシから作られる糖の混合物で、テンサイ(sugarbeet、甜菜、砂糖大根)やサトウキビ(sugarcane)から得られるしょ糖に似た味と甘さがある。この製造過程には3つの段階が必要で、それぞれ別々の酵素によって行われる。まずアミラーゼがでんぷんを小さな断片へと分解する。上図左(PDBエントリー 2taa )に示したような細菌のアミラーゼは、大量に得るのが簡単であるためよく用いられる。2つ目の段階は菌類のグルコアミラーゼ(glucoamylase、上図中央、PDBエントリー 1dog )によって行われる。この酵素は小さな断片を個々のグルコース単位へと分解する。ただ残念ながらグルコースは特にいい味がする訳ではないので、3つ目の段階を加えることになる。3つ目の段階はグルコースイソメラーゼ(glucose isomerase、グルコース異性化酵素)によって行われる。上図右(PDBエントリー 4xia )に示したこの酵素はキシロースイソメラーゼ(xylose isomerase)とも呼ばれる。この酵素はグルコースの一部をフルクトース(fructose、果糖)に変換して、ソフトドリンクからパワーバー(ネスレ社の栄養補給食品)まであらゆる食品に甘みを加えるのに用いられる甘い添加物を作り出す。しかし、この安くて広く用いられている甘味料は多少の欠点も伴うかもしれない。インターネットを検索すると、高果糖コーンシロップの摂りすぎが肥満(obesity)や糖尿病(diabetes)に果たす役割について議論が巻き起こっているのが分かるだろう。

(訳注)日本で原材料名の記載によく見られる「果糖ぶどう糖液糖」もこれと同類。「果糖ぶどう糖液糖」は異性化された糖(フルクトース)の含有率が50%以上90%未満の異性化液糖を指す(「異性化液糖及び砂糖混合異性化液糖の日本農業規格」による)。

構造をみる

α-アミラーゼ(PDB:1ppi) 灰色の球はカルシウムイオン、緑の球は塩化物イオン、黄と橙の分子は糖、ピンクは糖切断部位、右は左の活性部位を拡大表示したもの。

α-アミラーゼの活性部位は、その仕事の大半を担う3つの酸性基(赤と白で示した部分)を含んでいる。ここに示したアミラーゼ(PDBエントリー 1ppi )では、223番残基のグルタミン酸、197番のアスパラギン酸、300番のアスパラギン酸が一緒になって、でんぷん鎖中にある2つの糖の間の結合を切断する。この構造は、活性部位に結合している5つの糖単位でできた短い糖鎖(黄色と橙で示した部分)を含んでいる。そして切断部位はピンクで示している。大きな灰色の球で示したのはカルシウムイオンで、酵素の構造を安定化させている場所の近くに見られる。緑の球で示したのは塩化物イオンで、多くのアミラーゼにおいて活性部位の下部に結合し反応を助けている。

2006/02/03 にPDBでキーワード検索を行って決定した「alpha-amylase」に関係するPDBエントリーの一覧をこちらのリストに掲載しています。

2006/02/03 キーワード検索による関係PDBエントリー一覧
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PDB ID Title Authors Publication Year Journal Name Volume No First Page Pubmed ID
1amy Crystal and molecular structure of barley alpha-amylase. Kadziola, A., Abe, J., Svensson, B., Haser, R. 1994 J.Mol.Biol. 239 104 8196040
1aqh Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Aghajari, N., Feller, G., Gerday, C., Haser, R. 1998 Protein Sci. 7 564 9541387
1aqm
1b0i Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level. Aghajari, N., Feller, G., Gerday, C., Haser, R. 1998 Structure 6 1503 9862804
1jd7 Structural basis of alpha-amylase activation by chloride Aghajari, N., Feller, G., Gerday, C., Haser, R. 2002 Protein Sci. 11 1435 12021442
1jd9
1l0p Structural basis of alpha-amylase activation by chloride. Aghajari, N., Feller, G., Gerday, C., Haser, R. 2002 Protein Sci. 11 1435 12021442
1ava Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution. Vallee, F., Kadziola, A., Bourne, Y., Juy, M., Rodenburg, K.W., Svensson, B., Haser, R. 1998 Structure 6 649 9634702
1b1u Structure of the Bifunctional Inhibitor of Trypsin and Alpha-Amylase from Ragi Seeds at 2.2 Angstrom Resolution Gourinath, S., Srinivasan, A., Singh, T.P. 2000 Acta Crystallogr., Sect.D 55 287 10713515
1b2y 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. Qian, M., Haser, R., Buisson, G., Duee, E., Payan, F. 1994 Biochemistry 33 6284 8193143
1ppi
1bag Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose. Fujimoto, Z., Takase, K., Doui, N., Momma, M., Matsumoto, T., Mizuno, H. 1998 J.Mol.Biol. 277 393 9514750
1bea Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution. Behnke, C.A., Yee, V.C., Le Trong, I., Pedersen, L.C., Stenkamp, R.E., Kim, S.-S., Reeck, G.R., Teller, D.C. 1998 Biochemistry 37 15277 9799488
1bfa
1bfn Crystal structure of recombinant soybean beta-amylase complexed with beta-cyclodextrin. Adachi, M., Mikami, B., Katsube, T., Utsumi, S. 1998 J.Biol.Chem. 273 19859 9677422
1bg9 Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis. Kadziola, A., Sogaard, M., Svensson, B., Haser, R. 1998 J.Mol.Biol. 278 205 9571044
1bip Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy. Strobl, S., Muhlhahn, P., Bernstein, R., Wiltscheck, R., Maskos, K., Wunderlich, M., Huber, R., Glockshuber, R., Holak, T.A. 1995 Biochemistry 34 8281 7599120
1bli Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Machius, M., Declerck, N., Huber, R., Wiegand, G. 1998 Structure 6 281 9551551
1ob0 Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface. Machius, M., Declerck, N., Huber, R., Wiegand, G. 2003 J.Biol.Chem. 278 11546 12540849
1bpl Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution. Machius, M., Wiegand, G., Huber, R. 1995 J.Mol.Biol. 246 545 7877175
1bsi Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris. Rydberg, E.H., Sidhu, G., Vo, H.C., Hewitt, J., Cote, H.C., Wang, Y., Numao, S., MacGillivray, R.T., Overall, C.M., Brayer, G.D., Withers, S.G. 1999 Protein Sci. 8 635 10091666
1btc Three-dimensional structure of soybean beta-amylase determined at 3.0 A resolution: preliminary chain tracing of the complex with alpha-cyclodextrin. Mikami, B., Sato, M., Shibata, T., Hirose, M., Aibara, S., Katsube, Y., Morita, Y. 1992 J.Biochem.(Tokyo) 112 541 1491009
1bvn The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat. Wiegand, G., Epp, O., Huber, R. 1995 J.Mol.Biol. 247 99 7897663
1bvz Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution. Kamitori, S., Kondo, S., Okuyama, K., Yokota, T., Shimura, Y., Tonozuka, T., Sakano, Y. 1999 J.Mol.Biol. 287 907 10222200
1bya Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis. Mikami, B., Degano, M., Hehre, E.J., Sacchettini, J.C. 1994 Biochemistry 33 7779 8011643
1byb
1byc
1byd
1c8q Structure solution and refinment of recombinant human salivary amylase. Ramasubbu, N., Sekar, K., Velmurugan, D. n/a To be Published n/a n/a n/a
1clv Specific inhibition of insect alpha-amylases: yellow meal worm alpha-amylase in complex with the amaranth alpha-amylase inhibitor at 2.0 A resolution. Pereira, P.J., Lozanov, V., Patthy, A., Huber, R., Bode, W., Pongor, S., Strobl, S. 1999 Structure Fold.Des. 7 1079 10508777
1cpu Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques. Brayer, G.D., Sidhu, G., Maurus, R., Rydberg, E.H., Braun, C., Wang, Y., Nguyen, N.T., Overall, C.M., Withers, S.G. 2000 Biochemistry 39 4778 10769135
2cpu
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1cxk X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family. Uitdehaag, J.C., Mosi, R., Kalk, K.H., van der Veen, B.A., Dijkhuizen, L., Withers, S.G., Dijkstra, B.W. 1999 Nat. Struct. Biol. 6 432 10331869
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1d3c The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution. Uitdehaag, J.C., Kalk, K.H., van Der Veen, B.A., Dijkhuizen, L., Dijkstra, B.W. 1999 J.Biol.Chem. 274 34868 10574960
1dhk Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex. Bompard-Gilles, C., Rousseau, P., Rouge, P., Payan, F. 1996 Structure 4 1441 8994970
1dtu Rational design of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 to increase alpha-cyclodextrin production. van der Veen, B.A., Uitdehaag, J.C., Penninga, D., van Alebeek, G.J., Smith, L.M., Dijkstra, B.W., Dijkhuizen, L. 2000 J.Mol.Biol. 296 1027 10686101
1e3x Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes. Brzozowski, A.M., Lawson, D.M., Turkenburg, J.P., Bisgaard-Frantzen, H., Svendsen, A., Borchert, T.V., Dauter, Z., Wilson, K.S., Davies, G.J. 2000 Biochemistry 39 9099 10924103
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1e40
1e43
1eo5 Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity. Uitdehaag, J.C., van Alebeek, G.J., van Der Veen, B.A., Dijkhuizen, L., Dijkstra, B.W. 2000 Biochemistry 39 7772 10869182
1eo7
1esw X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cyclic glucans. Przylas, I., Terada, Y., Fujii, K., Takaha, T., Saenger, W., Strater, N. 2000 Eur. J. Biochem. 267 6903 11082203
1fp8 Structure and mechanism of the amylomaltase from Thermus thermophilus HB8 Uitdehaag, J.C.M., Euverink, G.J., van der Veen, B.A., van der Maarel, M., Dijkstra, B.W. n/a To be Published n/a n/a n/a
1fp9 Structure of the amylomaltase from Thermus thermophilus HB8 in space group C2 Uitdehaag, J.C.M., Euverink, G.J., van der Veen, B.A., van der Maarel, M., Dijkstra, B.W. n/a To be Published n/a n/a n/a
1g1y Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structure of the mutant E354A complexed with beta-cyclodextrin, and kinetic analyses on cyclodextrins. Kondo, S., Ohtaki, A., Tonozuka, T., Sakano, Y., Kamitori, S. 2001 J.Biochem.(Tokyo) 129 423 11226882
1g5a Amylosucrase, A Glucan-synthesizing Enzyme from the alpha-Amylase Family Skov, L.K., Mirza, O., Henriksen, A., De Montalk, G.P., Remaud-Simeon, M., Sarcabal, P., Willemot, R.M., Monsan, P., Gajhede, M. 2001 J.Biol.Chem. 276 25273 11306569
1g94 Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase. Aghajari, N., Roth, M., Haser, R. 2002 Biochemistry 41 4273 11914073
1g9h
1kxh
1gju The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity. Roujeinikova, A., Raasch, C., Burke, J., Baker, P.J., Liebl, W., Rice, D.W. 2001 J.Mol.Biol. 312 119 11545590
1gjw
1hny The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes. Brayer, G.D., Luo, Y., Withers, S.G. 1995 Protein Sci. 4 1730 8528071
1hoe Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A. Pflugrath, J.W., Wiegand, G., Huber, R., Vertesy, L. 1986 J.Mol.Biol. 189 383 3489104
1hss Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 A resolution. Oda, Y., Matsunaga, T., Fukuyama, K., Miyazaki, T., Morimoto, T. 1997 Biochemistry 36 13503 9354618
1ht6 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 Robert, X., Haser, R., Gottschalk, T.E., Ratajczak, F., Driguez, H., Svensson, B., Aghajari, N. 2003 Structure 11 973 12906828
1p6w
1htx Solution structure of the main alpha-amylase inhibitor from amaranth seeds. Martins, J.C., Enassar, M., Willem, R., Wieruzeski, J.M., Lippens, G., Wodak, S.J. 2001 Eur. J. Biochem. 268 2379 11298757
1hvx Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability. Suvd, D., Fujimoto, Z., Takase, K., Matsumura, M., Mizuno, H. 2001 J.Biol.Chem. 129 461 11226887
1hx0 Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex. Qian, M., Nahoum, V., Bonicel, J., Bischoff, H., Henrissat, B., Payan, F. 2001 Biochemistry 40 7700 11412124
1izj Mutual conversion of substrate specificities of Thermoactinomyces vulgaris R-47 alpha-amylases TVAI and TVAII by site-directed mutagenesis Ohtaki, A., Iguchi, A., Mizuno, M., Tonozuka, T., Sakano, Y., Kamitori, S. 2003 Carbohydr. Res. 338 1553 12860426
1izk
1j11 Crystal Structures of beta-Amylase from Bacillus cereus var. mycoides in Complexes with Substrate Analogs and Affinity-Labeling Reagents Oyama, T., Miyake, H., Kusunoki, M., Nitta, Y. 2003 J.Biochem.(Tokyo) 133 467 12761294
1j12
1jae Crystal structure of yellow meal worm alpha-amylase at 1.64 A resolution. Strobl, S., Maskos, K., Betz, M., Wiegand, G., Huber, R., Gomis-Ruth, F.X., Glockshuber, R. 1998 J.Mol.Biol. 278 617 9600843
1jf5 Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs Ohtaki, A., Kondo, S., Shimura, Y., Tonozuka, T., Sakano, Y., Kamitori, S. 2001 Carbohydr. Res. 334 309 11527532
1jf6
1jfh Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 A resolution. Qian, M., Spinelli, S., Driguez, H., Payan, F. 1997 Protein Sci. 6 2285 9385631
1ji1 Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution. Kamitori, S., Abe, A., Ohtaki, A., Kaji, A., Tonozuka, T., Sakano, Y. 2002 J.Mol.Biol. 318 443 12051850
1ji2
1jib Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues. Yokota, T., Tonozuka, T., Shimura, Y., Ichikawa, K., Kamitori, S., Sakano, Y. 2001 Biosci. Biotechnol. Biochem. 65 619 11330677
1jl8
1jxj Human salivary alpha-amylase Trp58 situated at subsite -2 is critical for enzyme activity. Ramasubbu, N., Ragunath, C., Mishra, P.J., Thomas, L.M., Kandra, L. 2004 Eur. J. Biochem. 271 2517 15182367
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1jxk Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase Ramasubbu, N., Ragunath, C., Mishra, P.J. 2003 J.Mol.Biol. 325 1061 12527308
1mfu Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. Ramasubbu, N., Ragunath, C., Mishra, P.J. 2003 J.Mol.Biol. 325 1061 12527308
1mfv
1kb3 Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase. Numao, S., Maurus, R., Sidhu, G., Wang, Y., Overall, C.M., Brayer, G.D., Withers, S.G. 2002 Biochemistry 41 215 11772019
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1kgw
1kgx
1kbb Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids. Rydberg, E.H., Li, C., Maurus, R., Overall, C.M., Brayer, G.D., Withers, S.G. 2002 Biochemistry 41 4492 11914097
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1kxq Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology. Desmyter, A., Spinelli, S., Payan, F., Lauwereys, M., Wyns, L., Muyldermans, S., Cambillau, C. 2002 J.Biol.Chem. 277 23645 11960990
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1lf6 Crystal structure and evolution of prokaryotic glucoamylase Aleshin, A.E., Feng, P.-H., Honzatko, R.B., Reilly, P.J. 2003 J.Mol.Biol. 327 61 12614608
1lf9
1lwh Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: implications for substrate specificity and catalysis. Roujeinikova, A., Raasch, C., Sedelnikova, S., Liebl, W., Rice, D.W. 2002 J.Mol.Biol. 321 149 12139940
1lwj
1mvy Oligosaccharide and Sucrose Complexes of Amylosucrase. Structural implications for the polymerase activity. Skov, L.K., Mirza, O., Sprogoe, D., Dar, I., Remaud-Simeon, M., Albenne, C., Monsan, P., Gajhede, M. 2002 J.Biol.Chem. 277 47741 12364331
1mw0 Oligosaccharide and sucrose complexes of amylosucrase. Structural implications for the polymerase activity. Skov, L.K., Mirza, O., Sprogoe, D., Dar, I., Remaud-Simeon, M., Albenne, C., Monsan, P., Gajhede, M. 2002 J.Biol.Chem. 277 47741 12364331
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1mwo Differential Regulation of a Hyperthermophilic alpha-Amylase with a Novel (Ca,Zn) Two-metal Center by Zinc Linden, A., Mayans, O., Meyer-Klaucke, W., Antranikian, G., Wilmanns, M. 2003 J.Biol.Chem. 278 9875 12482867
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1ok0 Crystal Structure of the Alpha-Amylase Inhibitor Tendamistat at 0.93 A Koenig, V., Vertesy, L., Schneider, T.R. 2003 Acta Crystallogr., Sect.D 59 1737 14501112
1ose Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose. Gilles, C., Astier, J.P., Marchis-Mouren, G., Cambillau, C., Payan, F. 1996 Eur. J. Biochem. 238 561 8681972
1ot1 The fully conserved Asp residue in Conserved sequence region I of the alpha-amylase Family is crucial for the Catalytic Site Architecture and Activity Leemhuis, H., Rozeboom, H.J., Dijkstra, B.W., Dijkhuizen, L. 2003 Febs Lett. 541 47 12706817
1ot2
1pif Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics. Machius, M., Vertesy, L., Huber, R., Wiegand, G. 1996 J.Mol.Biol. 260 409 8757803
1pig
1q4n Structural studies of a Phe256Trp mutant of human salivary alpha-amylase: implications for the role of a conserved water molecule in enzyme activity Ramasubbu, N., Sundar, K., Ragunath, C., Rafi, M.M. 2004 Arch. Biochem. Biophys. 421 115 14678792
1q6c Structural and Enzymatic Analysis of Soybean beta -Amylase Mutants with Increased pH Optimum Hirata, A., Adachi, M., Sekine, A., Kang, Y.N., Utsumi, S., Mikami, B. 2004 J.Biol.Chem. 279 7287 14638688
1q6d
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1q6g
1qfd Solution structure of the major alpha-amylase inhibitor of the crop plant amaranth. Lu, S., Deng, P., Liu, X., Luo, J., Han, R., Gu, X., Liang, S., Wang, X., Li, F., Lozanov, V., Patthy, A., Pongor, S. 1999 J.Biol.Chem. 274 20473 10400675
1qho X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution. Dauter, Z., Dauter, M., Brzozowski, A.M., Christensen, S., Borchert, T.V., Beier, L., Wilson, K.S., Davies, G.J. 1999 Biochemistry 38 8385 10387084
1qhp
1qi3 Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase. Hasegawa, K., Kubota, M., Matsuura, Y. 1999 Protein Eng. 12 819 10556241
1qi4
1qi5
1qpk
1qjv Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site Jenkins, J., Mayans, O., Smith, D., Worboys, K., Pickersgill, R. 2001 J.Mol.Biol. 305 951 11162105
1rp8 Oligosaccharide Binding to Barley alpha -Amylase 1 Robert, X., Haser, R., Mori, H., Svensson, B., Aghajari, N. 2005 J.Biol.Chem. 280 32968 16030022
1rp9
1rpk
1s46 Crystal structure of the covalent intermediate of amylosucrase from Neisseria polysaccharea. Jensen, M.H., Mirza, O., Albenne, C., Remaud-Simeon, M., Monsan, P., Gajhede, M., Skov, L.K. 2004 Biochemistry 43 3104 15023061
1smd Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity. Ramasubbu, N., Paloth, V., Luo, Y.G., Brayer, G.D., Levine, M.J. 1996 Acta Crystallogr., Sect.D 52 435 15299664
1tmq 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. Strobl, S., Maskos, K., Wiegand, G., Huber, R., Gomis-Ruth, F.X., Glockshuber, R. 1998 Structure 6 911 9687373
1u2y In Situ Extension as an Approach for Identifying Novel alpha-Amylase Inhibitors. Numao, S., Damager, I., Li, C., Wrodnigg, T.M., Begum, A., Overall, C.M., Brayer, G.D., Withers, S.G. 2004 J.Biol.Chem. 279 48282 15304511
1u30
1u33
1ua3 Crystal Structure of the Pig Pancreatic alpha-Amylase Complexed with Malto-Oligosaccharides Payan, F., Qian, M. 2003 J.Protein Chem. 22 275 12962327
1ua7 Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose Kagawa, M., Fujimoto, Z., Momma, M., Takase, K., Mizuno, H. 2003 J.Bacteriol. 185 6981 14617662
1ud2 Crystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) and its sodium ion binding sites Nonaka, T., Fujihashi, M., Kita, A., Hagihara, H., Ozaki, K., Ito, S., Miki, K. 2003 J.Biol.Chem. 278 24818 12719434
1ud3
1ud4
1ud5
1ud6
1ud8
1uh2 Complex Structures of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 with Malto-oligosaccharides Demonstrate the Role of Domain N Acting as a Starch-binding Domain Abe, A., Tonozuka, T., Sakano, Y., Kamitori, S. 2004 J.Mol.Biol. 335 811 14687576
1uh3
1uh4
1vah Crystal structure of the pig pancreatic alpha-amylase complexed with rho-nitrophenyl-alpha-D-maltoside-flexibility in the active site Zhuo, H., Payan, F., Qian, M. 2004 Protein J 23 379 15517985
1vb9 The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product Mizuno, M., Tonozuka, T., Uechi, A., Ohtaki, A., Ichikawa, K., Kamitori, S., Nishikawa, A., Sakano, Y. 2004 Eur. J. Biochem. 271 2530 15182368
1vfk Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism Ohtaki, A., Mizuno, M., Tonozuka, T., Sakano, Y., Kamitori, S. 2004 J.Biol.Chem. 279 31033 15138257
1vfm
1vfo
1vfu
1viw 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. Nahoum, V., Farisei, F., Le-Berre-Anton, V., Egloff, M.P., Rouge, P., Poerio, E., Payan, F. 1999 Acta Crystallogr., Sect.D 55 360 10089450
1vjs Crystal structure of thermostable alpha-amylase from Bacillus licheniformis refined at 1.7 A resolution Hwang, K.Y., Song, H.K., Chang, C., Lee, J., Lee, S.Y., Kim, K.K., Choe, S., Sweet, R.M., Suh, S.W. 1997 Mol.Cells 7 251 9163741
1w9x Structure of a Bacillus halmapalus family 13 alpha-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 A resolution. Davies, G., Brzozowski, A.M., Dauter, Z., Rasmussen, M.D., Borchert, T.V., Wilson, K.S. 2005 Acta Crystallogr., Sect.D 61 190 15681870
1wo2 Molecular Basis of the Effects of Chloride Ion on the Acid-Base Catalyst in the Mechanism of Pancreatic alpha-Amylase Qian, M., Ajandouz, E.H., Payan, F., Nahoum, V. 2005 Biochemistry 44 3194 15736930
1wp6 Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707 Kanai, R., Haga, K., Akiba, T., Yamane, K., Harata, K. 2004 Biochemistry 43 14047 15518553
1wpc
1wzk Mutagenesis and Structural Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase II (TVA II) Mizuno, M., Ichikawa, K., Tonozuka, T., Ohtaki, A., Shimura, Y., Kamitori, S., Nishikawa, A., Sakano, Y. n/a To be Published n/a n/a n/a
1wzl
1wzm
1xcw Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts Li, C., Begum, A., Numao, S., Park, K.H., Withers, S.G., Brayer, G.D. 2005 Biochemistry 44 3347 15736945
1xcx
1xd0
1xd1
1xgz Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase Maurus, R., Begum, A., Kuo, H.H., Racaza, A., Numao, S., Andersen, C., Tams, J.W., Vind, J., Overall, C.M., Withers, S.G., Brayer, G.D. 2005 Protein Sci. 14 743 15722449
1xh0
1xh1
1xh2
1xv8 Crystal Structure of Human Salivary Alpha-Amylase Dimer Fisher, S.Z., Govindasamy, L., Tu, C.K., Silverman, D.N., Rajaniemi, H., McKenna, R. n/a To be Published n/a n/a n/a
1z32 Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues Ramasubbu, N., Ragunath, C., Sundar, K., Mishra, P.J., Gyemant, G., Kandra, L. n/a To be Published n/a n/a n/a
2aaa Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus. Boel, E., Brady, L., Brzozowski, A.M., Derewenda, Z., Dodson, G.G., Jensen, V.J., Petersen, S.B., Swift, H., Thim, L., Woldike, H.F. 1990 Biochemistry 29 6244 2207069
2ait Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry. Kline, A.D., Braun, W., Wuthrich, K. 1988 J.Mol.Biol. 204 675 3265733
2bhu Crystal structure of maltooligosyltrehalose trehalohydrolase from Deinococcus radiodurans in complex with disaccharides. Timmins, J., Leiros, H.-K.S., Leonard, G., Leiros, I., Mcsweeney, S. 2005 J.Mol.Biol. 347 949 15784255
2bhy
2bhz
2c3g A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition. Boraston, A.B., Healey, M., Klassen, J., Ficko-Blean, E., Lammerts Van Bueren, A., Law, V. 2006 J.Biol.Chem. 281 587 16230347
2c3h
2c3v
2c3w
2c3x
2taa Structure and possible catalytic residues of Taka-amylase A Matsuura, Y., Kusunoki, M., Harada, W., Kakudo, M. 1984 J.Biochem.(Tokyo) 95 697 6609921
3ait Restrained Energy Refinement with Two Different Algorithms and Force Fields of the Structure of the Alpha-Amylase Inhibitor Tendamistat Determined by NMR in Solution Billeter, M., Schaumann, T., Braun, W., Wuthrich, K. 1990 Biopolymers 29 695 n/a
4ait
6taa Structure and molecular model refinement of Aspergillus oryzae (TAKA) alpha-amylase: an application of the simulated-annealing method. Swift, H.J., Brady, L., Derewenda, Z.S., Dodson, E.J., Dodson, G.G., Turkenburg, J.P., Wilkinson, A.J. 1991 Acta Crystallogr., Sect.B 47 535 1930835
7taa Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 A resolution. Brzozowski, A.M., Davies, G.J. 1997 Biochemistry 36 10837 9283074

α-アミラーゼについてさらに知りたい方へ

以下の参考文献もご参照ください。

  • E. A. MacGregor, S. Janecek and B. Svensson 2001 Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochimica et Biophysica Acta 1546 1-20
  • J. E. Nielsen and T. V. Borchert 2000 Protein engineering of bacterial alpha-amylases. Biochimica et Biophysica Acta 1543 253-274



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2006-02-01 (last edited: 7 months ago)2016-09-09
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