Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution. - Wikidata - awgldk - TriplyDB

Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution.

Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution.

http://www.wikidata.org/entity/Q50104392

about

Computational protein engineering: bridging the gap between rational design and laboratory evolution.Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis.Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily.Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.CADEE: Computer-Aided Directed Evolution of Enzymes.Stabilization of different types of transition states in a single enzyme active site: QM/MM analysis of enzymes in the alkaline phosphatase superfamily.Why nature really chose phosphate.The logic of metabolism and its fuzzy consequences.Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase Superfamily Modeling catalytic promiscuity in the alkaline phosphatase superfamily.Role of Conformational Dynamics in the Evolution of Retro-Aldolase Activity.

P2860

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P2860

Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution.

http://www.wikidata.org/entity/Q50104392

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

@zh-my

2012年学术文章

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2012年學術文章

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2012年學術文章

@zh-hant

name

Catalytic promiscuity in Pseud ...... stry-driven protein evolution.

@en

Catalytic promiscuity in Pseud ...... stry-driven protein evolution.

@nl

type

label

Catalytic promiscuity in Pseud ...... stry-driven protein evolution.

@en

Catalytic promiscuity in Pseud ...... stry-driven protein evolution.

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prefLabel

Catalytic promiscuity in Pseud ...... stry-driven protein evolution.

@en

Catalytic promiscuity in Pseud ...... stry-driven protein evolution.

@nl

P1433

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P356

J.FEBSLET.2012.04.012

P1433

P1476

Catalytic promiscuity in Pseud ...... stry-driven protein evolution.

@en

P2860

The Protein Data Bank

Electrostatic basis for enzyme catalysis

Efficient catalytic promiscuity in an enzyme superfamily: an arylsulfatase shows a rate acceleration of 10(13) for phosphate monoester hydrolysis

Enzyme recruitment in evolution of new function

Mechanistic alternatives in phosphate monoester hydrolysis: what conclusions can be drawn from available experimental data?

Enzyme promiscuity: a mechanistic and evolutionary perspective.

Examining the promiscuous phosphatase activity of Pseudomonas aeruginosa arylsulfatase: a comparison to analogous phosphatases.

QM/MM analysis suggests that Alkaline Phosphatase (AP) and nucleotide pyrophosphatase/phosphodiesterase slightly tighten the transition state for phosphate diester hydrolysis relative to solution: implication for catalytic promiscuity in the AP supe

Isotope effects in the study of phosphoryl and sulfuryl transfer reactions.

Energetics of enzyme catalysis.

P304

1622-1630

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.FEBSLET.2012.04.012

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P433

11

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586

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Shina Caroline Lynn Kamerlin

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2012-04-25T00:00:00Z

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P5875

225278751

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22673572

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P921

protein evolution