(Q43029042)

English

Residues at the active site of the esterase 2 from Alicyclobacillus acidocaldarius involved in substrate specificity and catalytic activity at high temperature

scientific article published on 10 July 2001

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scholarly article

1 reference

Europe PubMed Central

12 November 2017

Residues at the active site of the esterase 2 from Alicyclobacillus acidocaldarius involved in substrate specificity and catalytic activity at high temperature (English)

1 reference

Europe PubMed Central

12 November 2017

1

1 reference

Europe PubMed Central

12 November 2017

author name string

Mandrich L

2

1 reference

Europe PubMed Central

12 November 2017

Rossi M

3

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Europe PubMed Central

12 November 2017

language of work or name

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publication date

10 July 2001

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Europe PubMed Central

12 November 2017

Journal of Biological Chemistry

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Europe PubMed Central

12 November 2017

276

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Europe PubMed Central

12 November 2017

40

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Europe PubMed Central

12 November 2017

37482-37490

1 reference

Europe PubMed Central

12 November 2017

Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid

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Homology modeling and active-site residues probing of the thermophilic Alicyclobacillus acidocaldarius esterase 2.

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Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase

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The alpha/beta hydrolase fold

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The thermophilic esterase from Archaeoglobus fulgidus: structure and conformational dynamics at high temperature.

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

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Proteins and temperature

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Directed evolution of a thermostable esterase.

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A structural view of evolutionary divergence

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Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases

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Directed evolution study of temperature adaptation in a psychrophilic enzyme

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Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution

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Identifiers

10.1074/JBC.M103017200

1 reference

Europe PubMed Central

12 November 2017

1 reference

Europe PubMed Central

12 November 2017

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