A new member of the alkaline phosphatase superfamily with a formylglycine nucleophile: structural and kinetic characterisation of a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum

A new member of the alkaline phosphatase superfamily with a formylglycine nucleophile: structural and kinetic characterisation of a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum

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http://www.wikidata.org/entity/Q27652157

Q27652157

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Distinct and essential morphogenic functions for wall- and lipo-teichoic acids in Bacillus subtilis An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily Computational protein engineering: bridging the gap between rational design and laboratory evolution.Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states 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 Site-directed mutagenesis maps interactions that enhance cognate and limit promiscuous catalysis by an alkaline phosphatase superfamily phosphodiesterase.Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily.Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Matching the Diversity of Sulfated Biomolecules: Creation of a Classification Database for Sulfatases Reflecting Their Substrate Specificity.Specificity Effects of Amino Acid Substitutions in Promiscuous Hydrolases: Context-Dependence of Catalytic Residue Contributions to Local Fitness Landscapes in Nearby Sequence Space.High resolution crystal structure of the catalytic domain of MCR-1.Insights into the Mechanistic Basis of Plasmid-Mediated Colistin Resistance from Crystal Structures of the Catalytic Domain of MCR-1 Root traits and microbial community interactions in relation to phosphorus availability and acquisition, with particular reference to Brassica.Copper is a Cofactor of the Formylglycine-Generating Enzyme Why nature really chose phosphate.Microbial alkyl- and aryl-sulfatases: mechanism, occurrence, screening and stereoselectivities.Microevolution Analysis of Bacillus coahuilensis Unveils Differences in Phosphorus Acquisition Strategies and Their Regulation.Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.Heterologous expression in Pichia pastoris and biochemical characterization of the unmodified sulfatase from Fusarium proliferatum LE1.Detection, production, and application of microbial arylsulfatases.Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase Superfamily Modeling catalytic promiscuity in the alkaline phosphatase superfamily.Kinetic and computational evidence for an intermediate in the hydrolysis of sulfonate esters.Isolation and Characterization of Bacteria That Degrade Phosphonates in Marine Dissolved Organic Matter.Differential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.Mutation of Conserved Residues Increases in Vitro Activity of the Formylglycine-Generating Enzyme.Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme.Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester.Homologous expression and biochemical characterization of the arylsulfatase from Kluyveromyces lactis and its relevance in milk processing.Catalytic mechanism of the arylsulfatase promiscuous enzyme from Pseudomonas aeruginosa.

P2860

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P2860

A new member of the alkaline phosphatase superfamily with a formylglycine nucleophile: structural and kinetic characterisation of a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum

Item

http://www.wikidata.org/entity/Q27652157

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2008 nî lūn-bûn

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2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

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