Literature DB >> 11898334

Biochemical confirmation and characterization of the family-57-like alpha-amylase of Methanococcus jannaschii.

J W Kim1, L O Flowers, M Whiteley, T L Peeples.   

Abstract

The gene encoding a family-57-like alpha-amylase in the hyperthermophilic archaeon Methanococcus jannaschii, has been cloned into Escherichia coli. Extremely thermoactive alpha-amylase was confirmed in partially purified enzyme solution of the recombinant culture. This enzyme activity had a temperature optimum of 120 degrees C and a pH optimum 5.0-8.0. The amylase activity is extremely stable against denaturants. Hydrolysis of large sugar polymers with alpha-1-6 and alpha-1-4 linkages yields products including glucose polymers of 1-7 units. Highest activity is exhibited on amylose. The catalyst exhibited a half-life of 50 h at 100 degrees C, among the highest reported thermostabilities of natural amylases.

Entities:  

Mesh：

Substances：

Year:  2001        PMID： 11898334     DOI： 10.1007/bf02817988

Source DB:  PubMed          Journal:  Folia Microbiol (Praha)        ISSN： 0015-5632            Impact factor:   2.099


  17 in total

1.  Close evolutionary relatedness of alpha-amylases from Archaea and plants.

Authors:  S Janecek; E Lévêque; A Belarbi; B Haye
Journal:  J Mol Evol       Date:  1999-04       Impact factor: 2.395

2.  Novel, thermostable family-13-like glycoside hydrolase from Methanococcus jannaschii.

Authors:  J W Kim; H A Terc; L O Flowers; M Whiteley; T L Peeples
Journal:  Folia Microbiol (Praha)       Date:  2001       Impact factor: 2.099

3.  Characterization of Amylolytic Enzyme Activities Associated with the Hyperthermophilic Archaebacterium Pyrococcus furiosus.

Authors:  S H Brown; H R Costantino; R M Kelly
Journal:  Appl Environ Microbiol       Date:  1990-07       Impact factor: 4.792

Review 4.  Glycosyl hydrolases from hyperthermophilic microorganisms.

Authors:  M W Bauer; L E Driskill; R M Kelly
Journal:  Curr Opin Biotechnol       Date:  1998-04       Impact factor: 9.740

5.  Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme.

Authors:  G Dong; C Vieille; A Savchenko; J G Zeikus
Journal:  Appl Environ Microbiol       Date:  1997-09       Impact factor: 4.792

6.  Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme.

Authors:  G Dong; C Vieille; J G Zeikus
Journal:  Appl Environ Microbiol       Date:  1997-09       Impact factor: 4.792

7.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

8.  The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus.

Authors:  K A Laderman; B R Davis; H C Krutzsch; M S Lewis; Y V Griko; P L Privalov; C B Anfinsen
Journal:  J Biol Chem       Date:  1993-11-15       Impact factor: 5.157

9.  Sequence of archaeal Methanococcus jannaschii alpha-amylase contains features of families 13 and 57 of glycosyl hydrolases: a trace of their common ancestor?

Authors:  S Janecek
Journal:  Folia Microbiol (Praha)       Date:  1998       Impact factor: 2.099

10.  Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity.

Authors:  G Buisson; E Duée; R Haser; F Payan
Journal:  EMBO J       Date:  1987-12-20       Impact factor: 11.598
View more
  10 in total

1.  Novel, thermostable family-13-like glycoside hydrolase from Methanococcus jannaschii.

Authors:  J W Kim; H A Terc; L O Flowers; M Whiteley; T L Peeples
Journal:  Folia Microbiol (Praha)       Date:  2001       Impact factor: 2.099

2.  Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57.

Authors:  Karol Blesák; Stefan Janeček
Journal:  Extremophiles       Date:  2012-04-22       Impact factor: 2.395

3.  A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.

Authors:  Taira Murakami; Tamotsu Kanai; Hiroki Takata; Takashi Kuriki; Tadayuki Imanaka
Journal:  J Bacteriol       Date:  2006-08       Impact factor: 3.490

4.  Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues.

Authors:  Stefan Janeček; Karol Blesák
Journal:  Protein J       Date:  2011-08       Impact factor: 2.371

Review 5.  α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.

Authors:  Štefan Janeček; Birte Svensson; E Ann MacGregor
Journal:  Cell Mol Life Sci       Date:  2013-06-27       Impact factor: 9.261

Review 6.  Review: Engineering of thermostable enzymes for industrial applications.

Authors:  Federica Rigoldi; Stefano Donini; Alberto Redaelli; Emilio Parisini; Alfonso Gautieri
Journal:  APL Bioeng       Date:  2018-01-11

Review 7.  Deep Hypersaline Anoxic Basins as Untapped Reservoir of Polyextremophilic Prokaryotes of Biotechnological Interest.

Authors:  Stefano Varrella; Michael Tangherlini; Cinzia Corinaldesi
Journal:  Mar Drugs       Date:  2020-01-30       Impact factor: 5.118

Review 8.  Glycoside Hydrolases and Glycosyltransferases from Hyperthermophilic Archaea: Insights on Their Characteristics and Applications in Biotechnology.

Authors:  Khadija Amin; Sylvain Tranchimand; Thierry Benvegnu; Ziad Abdel-Razzak; Hala Chamieh
Journal:  Biomolecules       Date:  2021-10-21

9.  In silico analysis of the α-amylase family GH57: eventual subfamilies reflecting enzyme specificities.

Authors:  Mária Martinovičová; Štefan Janeček
Journal:  3 Biotech       Date:  2018-07-09       Impact factor: 2.406

Review 10.  Biotechnological applications of archaeal enzymes from extreme environments.

Authors:  Ma Ángeles Cabrera; Jenny M Blamey
Journal:  Biol Res       Date:  2018-10-05       Impact factor: 5.612
  10 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.