(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

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Europe PubMed Central

PubMed publication ID

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

PubMed publication ID

12 November 2017

1

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Europe PubMed Central

PubMed publication ID

12 November 2017

author name string

Mandrich L

2

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Europe PubMed Central

PubMed publication ID

12 November 2017

Rossi M

3

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Europe PubMed Central

PubMed publication ID

12 November 2017

language of work or name

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publication date

10 July 2001

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Europe PubMed Central

PubMed publication ID

12 November 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

12 November 2017

276

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Europe PubMed Central

PubMed publication ID

12 November 2017

40

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Europe PubMed Central

PubMed publication ID

12 November 2017

37482-37490

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

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

1 reference

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

1 reference

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

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

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The esterase from the thermophilic eubacterium Bacillus acidocaldarius: structural-functional relationship and comparison with the esterase from the hyperthermophilic archaeon Archaeoglobus fulgidus.

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Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey

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Patterns of temperature adaptation in proteins from Methanococcus and Bacillus

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Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species

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Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability

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Enzyme engineering reaches the boiling point

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

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21 January 2018

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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21 January 2018

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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Engineering an enzyme to resist boiling

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Enhancement of the enzymatic activity of ribonuclease HI from Thermus thermophilus HB8 with a suppressor mutation method

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Identifiers

10.1074/JBC.M103017200

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

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