(Q33864977)

English

Revisiting the lipase from Pseudomonas aeruginosa: directed evolution of substrate acceptance and enantioselectivity using iterative saturation mutagenesis

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scholarly article

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Europe PubMed Central

PubMed publication ID

29 July 2017

Revisiting the lipase from Pseudomonas aeruginosa: directed evolution of substrate acceptance and enantioselectivity using iterative saturation mutagenesis (English)

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

directed evolution

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enantioselectivity

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based on heuristic

inferred from title

Pseudomonas aeruginosa

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based on heuristic

inferred from title

Manfred T. Reetz

3

object named as

Manfred T Reetz

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Europe PubMed Central

PubMed publication ID

29 July 2017

author name string

Shreenath Prasad

1

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Europe PubMed Central

PubMed publication ID

29 July 2017

Marco Bocola

2

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Europe PubMed Central

PubMed publication ID

29 July 2017

publication date

5 April 2011

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Europe PubMed Central

PubMed publication ID

29 July 2017

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

12

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Europe PubMed Central

PubMed publication ID

29 July 2017

8

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

1550-1557

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Europe PubMed Central

PubMed publication ID

29 July 2017

Laboratory evolution of stereoselective enzymes: a prolific source of catalysts for asymmetric reactions

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Exploring protein fitness landscapes by directed evolution

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Protein Design by Directed Evolution

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Advances in laboratory evolution of enzymes

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Enzyme engineering for enantioselectivity: from trial-and-error to rational design?

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Advances in generating functional diversity for directed protein evolution.

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Screening and selection methods for large-scale analysis of protein function

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Selection strategies for improved biocatalysts

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Investigating and Engineering Enzymes by Genetic Selection

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A genetic selection system for evolving enantioselectivity of enzymes

1 reference

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Novel methods for directed evolution of enzymes: quality, not quantity

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Enzyme optimization: moving from blind evolution to statistical exploration of sequence-function space

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Rational assignment of key motifs for function guides in silico enzyme identification

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Addressing the numbers problem in directed evolution

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Mutants generated by the insertion of random oligonucleotides into the active site of the beta-lactamase gene

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Laboratory evolution of robust and enantioselective Baeyer-Villiger monooxygenases for asymmetric catalysis

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Induced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase

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Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes

1 reference

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Iterative saturation mutagenesis accelerates laboratory evolution of enzyme stereoselectivity: rigorous comparison with traditional methods.

1 reference

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Controlling the enantioselectivity of enzymes by directed evolution: practical and theoretical ramifications

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Expanding the substrate scope of enzymes: combining mutations obtained by CASTing

1 reference

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Crystal structure of pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases

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Learning from directed evolution: Further lessons from theoretical investigations into cooperative mutations in lipase enantioselectivity

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Making optimal use of empirical energy functions: force-field parameterization in crystal space

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Improved PCR method for the creation of saturation mutagenesis libraries in directed evolution: application to difficult-to-amplify templates

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A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations

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Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation

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Fast empirical pKa prediction by Ewald summation.

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Protein engineering of the high-alkaline serine protease PB92 from Bacillus alcalophilus: functional and structural consequences of mutation at the S4 substrate binding pocket

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Directed evolution of enantioselective enzymes: iterative cycles of CASTing for probing protein-sequence space

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Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability

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Directed Evolution of an Enantioselective Enzyme through Combinatorial Multiple-Cassette Mutagenesis

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Directed evolution of an enantioselective lipase with broad substrate scope for hydrolysis of alpha-substituted esters

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Expanding the range of substrate acceptance of enzymes: combinatorial active-site saturation test

1 reference

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Electroporation of freshly plated Escherichia coli and Pseudomonas aeruginosa cells

1 reference

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A smooth particle mesh Ewald method

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inferred from DOI database lookup

Identifiers

10.1002/CPHC.201100031

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

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