(Q56901872)

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Enzyme evolution. Design by necessity

scientific article published in Nature

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title

Enzyme evolution. Design by necessity (English)

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1

G A Petsko

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language of work or name

English

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publication date

10 February 2000

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published in

Nature

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volume

403

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page(s)

606-7

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issue

6770

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exact match

https://scigraph.springernature.com/pub.10.1038/35001176

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cites work

Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold

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Characterization of a helical protein designed from first principles

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De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence

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21 January 2018

Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis.

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21 January 2018

Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase.

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Directed evolution converts subtilisin E into a functional equivalent of thermitase

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Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation

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Directed evolution of biocatalysts

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On the origin of enzymatic species

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The evolution of alpha/beta barrel enzymes

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Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

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Protein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop

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Rapid evolution of a protein in vitro by DNA shuffling

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Identifiers

DOI

10.1038/35001176

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Dimensions Publication ID

1037497716

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PubMed ID

10688181

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(Q56901872)

Enzyme evolution. Design by necessity

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