Biological chemistry: enzymes in focus. - Wikidata - awgldk - TriplyDB

Biological chemistry: enzymes in focus.

Biological chemistry: enzymes in focus.

http://www.wikidata.org/entity/Q51366804

about

Biological chemistry: enzymes in focus.

http://www.wikidata.org/entity/Q51366804

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh-hant

name

Biological chemistry: enzymes in focus.

@en

Biological chemistry: enzymes in focus.

@nl

type

label

Biological chemistry: enzymes in focus.

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Biological chemistry: enzymes in focus.

@nl

prefLabel

Biological chemistry: enzymes in focus.

@en

Biological chemistry: enzymes in focus.

@nl

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Biological chemistry: enzymes in focus.

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P2860

Inverting enantioselectivity of Burkholderia cepacia KWI-56 lipase by combinatorial mutation and high-throughput screening using single-molecule PCR and in vitro expression.

Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site.

Rational evolution of a medium chain-specific cytochrome P-450 BM-3 variant.

Cassette mutagenesis: an efficient method for generation of multiple mutations at defined sites.

Improving enzyme properties: when are closer mutations better?

Engineering delta 9-16:0-acyl carrier protein (ACP) desaturase specificity based on combinatorial saturation mutagenesis and logical redesign of the castor delta 9-18:0-ACP desaturase.

Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenylbutyrate.

Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than distant mutations.

Directed evolution of an enantioselective lipase

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1096-1097

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scholarly article

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10.1038/4361096A

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7054

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436

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Romas J. Kazlauskas

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2005-08-01T00:00:00Z

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1011634337

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16121163

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