Bioinformatic and biochemical analysis of a novel maltose-forming α-amylase of the GH57 family in the hyperthermophilic archaeon Thermococcus sp. CL1-Reference-Cited by-同舟云学术

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Bioinformatic and biochemical analysis of a novel maltose-forming α-amylase of the GH57 family in the hyperthermophilic archaeon Thermococcus sp. CL1

Published:2014-06 Issue: Volume:60 Page:9-15
ISSN:0141-0229
Container-title:Enzyme and Microbial Technology
language:en
Short-container-title:Enzyme and Microbial Technology

Author:

Jeon Eun-Jung,Jung Jong-Hyun,Seo Dong-Ho,Jung Dong-Hyun,Holden James F.,Park Cheon-Seok

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Biochemistry,Biotechnology,Bioengineering

Reference34 articles.

1. Starch modification with microbial α-glucanotransferase enzymes;van der Maarel;Carbohydr Polym,2013

2. Starch-hydrolyzing enzymes from thermophilic archaea and bacteria;Bertoldo;Curr Opin Chem Biol,2002

3. α-Amylase: an enzyme specificity found in various families of glycoside hydrolases;Janeček;Cell Mol Life Sci,2014

4. Structure and possible catalytic residues of Taka-amylase A;Matsuura;J Biochem,1984

5. Crystal structures of 4-α-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor;Imamura;J Biol Chem,2003

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1. Protein secretion zones during overexpression of amylase within the Gram-positive cell wall;BMC Biology;2023-10-04

2. Molecular cloning and production of recombinant Pcal_0672, a family GH57 glycoside hydrolase from Pyrobaculum calidifontis;Biologia;2023-03-09

3. Sequence-structural features and evolution of the α-amylase family GH119 revealed by the in silico analysis of its relatedness to the family GH57;Biologia;2023-03-06

4. Industrial applications of thermophilic/hyperthermophilic enzymes;Developments and Applications of Enzymes from Thermophilic Microorganisms;2023

5. Acceptor dependent catalytic properties of GH57 4-α-glucanotransferase from Pyrococcus sp. ST04;Frontiers in Microbiology;2022-10-06

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