Activity-stability relationships in extremophilic enzymes (Q43032163)

12 November 2017

Activity-stability relationships in extremophilic enzymes (English)

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12 November 2017

Salvino D'Amico

1

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12 November 2017

Jean-Claude Marx

series ordinal

2

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12 November 2017

Charles Gerday

series ordinal

3

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12 November 2017

Georges Feller

series ordinal

4

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12 November 2017

language of work or name

English

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publication date

2 January 2003

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Journal of Biological Chemistry

12 November 2017

6

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based on heuristic

inferred from page(s)

published in

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12 November 2017

278

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12 November 2017

10

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12 November 2017

7891-7896

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Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability

12 November 2017

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https://api.crossref.org/works/10.1074%2FJBC.M212508200

Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper temperature limit for life to 113 degrees C.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Psychrophiles and polar regions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Molecular basis of cold adaptation.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M212508200

Temperature adaptation of enzymes: lessons from laboratory evolution

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M212508200

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M212508200

Toward a molecular understanding of cold activity of enzymes from psychrophiles

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

21 January 2018

Cold adapted enzymes.

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https://api.crossref.org/works/10.1074%2FJBC.M212508200

Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Activity and stability of a thermostable alpha-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Determination and analysis of urea and guanidine hydrochloride denaturation curves

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Non-detergent sulphobetaines: a new class of mild solubilization agents for protein purification

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Maximal stabilities of reversible two-state proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Thermodynamic differences among homologous thermophilic and mesophilic proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Cold denaturation of proteins

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M212508200

Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Review: Protein function at thermal extremes: balancing stability and flexibility

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

A better enzyme to cope with cold. Comparative flexibility studies on psychrotrophic, mesophilic, and thermophilic IPMDHs.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Temperature adaptation of enzymes: roles of the free energy, the enthalpy, and the entropy of activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

From Levinthal to pathways to funnels

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

The fundamentals of protein folding: bringing together theory and experiment

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Understanding protein folding via free-energy surfaces from theory and experiment

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Folding and binding cascades: shifts in energy landscapes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Folding and binding cascades: dynamic landscapes and population shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

Transition-state ensemble in enzyme catalysis: possibility, reality, or necessity?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212508200

21 January 2018

Identifiers

DOI

10.1074/JBC.M212508200

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12 November 2017

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