Site-directed mutagenesis maps interactions that enhance cognate and limit promiscuous catalysis by an alkaline phosphatase superfamily phosphodiesterase.
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Specificity Effects of Amino Acid Substitutions in Promiscuous Hydrolases: Context-Dependence of Catalytic Residue Contributions to Local Fitness Landscapes in Nearby Sequence Space.Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Characterization of Wall Teichoic Acid Degradation by the Bacteriophage ϕ29 Appendage Protein GP12 Using Synthetic Substrate Analogs.Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase SuperfamilyDifferential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.Evolutionary repurposing of a sulfatase: A new Michaelis complex leads to efficient transition state charge offset
P2860
Site-directed mutagenesis maps interactions that enhance cognate and limit promiscuous catalysis by an alkaline phosphatase superfamily phosphodiesterase.
description
2013 nî lūn-bûn
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2013年の論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年论文
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2013年论文
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2013年论文
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name
Site-directed mutagenesis maps ...... superfamily phosphodiesterase.
@ast
Site-directed mutagenesis maps ...... superfamily phosphodiesterase.
@en
type
label
Site-directed mutagenesis maps ...... superfamily phosphodiesterase.
@ast
Site-directed mutagenesis maps ...... superfamily phosphodiesterase.
@en
prefLabel
Site-directed mutagenesis maps ...... superfamily phosphodiesterase.
@ast
Site-directed mutagenesis maps ...... superfamily phosphodiesterase.
@en
P2093
P2860
P356
P1433
P1476
Site-directed mutagenesis maps ...... superfamily phosphodiesterase.
@en
P2093
Daniel Herschlag
Fanny Sunden
Helen Wiersma-Koch
P2860
P304
P356
10.1021/BI4010045
P407
P577
2013-12-11T00:00:00Z