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Bioscience, Biotechnology, and Biochemistry Volume 62, 1998 - Issue 6
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Original Articles

Clustered Proline Residues around the Active-Site Cleft in Thermostable Oligo-1,6-glucosidase of Bacillus flavocaldarius KP1228

Shin-ichi KASHIWABARALaboratory of Microbial Physiology and Applied Microbiology, Department of Applied Biochemistry, Kyoto Prefectural University
,
Yoshifumi MATSUKILaboratory of Microbial Physiology and Applied Microbiology, Department of Applied Biochemistry, Kyoto Prefectural University
,
Takahide KISHIMOTOLaboratory of Microbial Physiology and Applied Microbiology, Department of Applied Biochemistry, Kyoto Prefectural University
&
Yuzuru SUZUKILaboratory of Microbial Physiology and Applied Microbiology, Department of Applied Biochemistry, Kyoto Prefectural University
Pages 1093-1102 | Received 30 Oct 1997, Published online: 22 May 2014

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Katsuichiro OKAZAKI, Takashi AMANO, Tetsuhiro MORIMOTO, Takahiro IEMOTO, Toshiyuki KAWABATA, Shigeru HAYAKAWA & Kazuya AKIMITSU. (2001) Cloning and Nucleotide Sequence of the Mycodextranase Gene from Streptomyces sp. J-13-3. Bioscience, Biotechnology, and Biochemistry 65:7, pages 1684-1687.
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Articles from other publishers (10)

Yana Y. Berlina, Lada E. Petrovskaya, Elena A. Kryukova, Lyudmila N. Shingarova, Sultan Sh. Gapizov, Mariya V. Kryukova, Elizaveta M. Rivkina, Mikhail P. Kirpichnikov & Dmitry A. Dolgikh. (2021) Engineering of Thermal Stability in a Cold-Active Oligo-1,6-Glucosidase from Exiguobacterium sibiricum with Unusual Amino Acid Content. Biomolecules 11:8, pages 1229.
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Zixing Dong, Cunduo Tang, Yunfeng Lu, Lunguang Yao & Yunchao Kan. (2019) Microbial Oligo‐α‐1,6‐Glucosidase: Current Developments and Future Perspectives. Starch - Stärke 72:1-2, pages 1900172.
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Zixing Dong, Xiaoming Hao, Daman S. Pokhrel, Xiaoling Chen, Xiaoguang Liu, Nokuthula P. Mchunu, Kugenthiren Permaul, Suren Singh, Dandan Niu & Zhengxiang Wang. (2018) Molecular cloning and biochemical characterization of two novel oligo-1,6-glucosidases from Bacillus mycoides and Thermomyces lanuginosus . Starch - Stärke 70:1-2, pages 1700093.
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Katarína Majzlová, Zuzana Pukajová & Štefan Janeček. (2013) Tracing the evolution of the α-amylase subfamily GH13_36 covering the amylolytic enzymes intermediate between oligo-1,6-glucosidases and neopullulanases. Carbohydrate Research 367, pages 48-57.
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Keizo Yamamoto, Hideo Miyake, Masami Kusunoki & Shigeyoshi Osaki. (2010) Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose . The FEBS Journal 277:20, pages 4205-4214.
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Cheng Zhou, Yanfen Xue & Yanhe Ma. (2010) Enhancing the thermostability of α-glucosidase from Thermoanaerobacter tengcongensis MB4 by single proline substitution. Journal of Bioscience and Bioengineering 110:1, pages 12-17.
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Keizo Yamamoto, Akifumi Nakayama, Yuka Yamamoto & Shiro Tabata. (2004) Val216 decides the substrate specificity of α‐glucosidase in Saccharomyces cerevisiae . European Journal of Biochemistry 271:16, pages 3414-3420.
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Yuzuru Suzuki. 2003. Enzyme Functionality. Enzyme Functionality.
E.Ann MacGregor, Štefan Janeček & Birte Svensson. (2001) Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1546:1, pages 1-20.
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D. Georlette, Z. O. Jónsson, F. Van Petegem, J.-P. Chessa, J. Van Beeumen, U. Hübscher & C. Gerday. (2000) A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. European Journal of Biochemistry 267:12, pages 3502-3512.
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