Literature DB >> 7858973

Thermostability and thermoactivity of enzymes from hyperthermophilic Archaea.

M W Adams1, R M Kelly.   

Abstract

Enzymes from hyperthermophilic microorganisms are characteristically thermostable and thermoactive at extremely high temperatures. Information about the basis for the structure and function of these novel proteins is beginning to emerge. However, there are very few generalizations that can be drawn at this point that can be derived from the limited number of studies that have focused on biocatalysis and thermostability at extremely high temperatures.

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Year:  1994        PMID: 7858973     DOI: 10.1016/0968-0896(94)85015-1

Source DB:  PubMed          Journal:  Bioorg Med Chem        ISSN: 0968-0896            Impact factor:   3.641


  4 in total

1.  Purification and Characterization of Two Functional Forms of Intracellular Protease PfpI from the Hyperthermophilic Archaeon Pyrococcus furiosus.

Authors:  S B Halio; M W Bauer; S Mukund; M Adams; R M Kelly
Journal:  Appl Environ Microbiol       Date:  1997-01       Impact factor: 4.792

2.  Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus.

Authors:  S B Halio; I I Blumentals; S A Short; B M Merrill; R M Kelly
Journal:  J Bacteriol       Date:  1996-05       Impact factor: 3.490

Review 3.  Physiological limits to life in anoxic subseafloor sediment.

Authors:  William D Orsi; Bernhard Schink; Wolfgang Buckel; William F Martin
Journal:  FEMS Microbiol Rev       Date:  2020-03-01       Impact factor: 16.408

4.  xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana.

Authors:  C Vieille; J M Hess; R M Kelly; J G Zeikus
Journal:  Appl Environ Microbiol       Date:  1995-05       Impact factor: 4.792

  4 in total

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