Crystal structure of Klebsiella sp. ASR1 phytase suggests substrate binding to a preformed active site that meets the requirements of a plant rhizosphere enzyme

Crystal structure of Klebsiella sp. ASR1 phytase suggests substrate binding to a preformed active site that meets the requirements of a plant rhizosphere enzyme

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http://www.wikidata.org/entity/Q27660528
Degradation of Phytate by the 6-Phytase from Hafnia alvei: A Combined Structural and Solution StudyMechanism of Protein Kinetic Stabilization by Engineered Disulfide CrosslinksStructural and biochemical analysis of a unique phosphatase from Bdellovibrio bacteriovorus reveals its structural and functional relationship with the protein tyrosine phosphatase class of phytaseDiet shapes the ability of human intestinal microbiota to degrade phytate- in vitrostudiesDirected evolution of a highly active Yersinia mollaretii phytase.Novel Glucose-1-Phosphatase with High Phytase Activity and Unusual Metal Ion Activation from Soil Bacterium Pantoea sp. Strain 3.5.1.High-quality draft genome sequence of a new phytase-producing microorganism Pantoea sp. 3.5.1.Engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency.Identification and characterization of a mesophilic phytase highly resilient to high-temperatures from a fungus-garden associated metagenome.Iterative key-residues interrogation of a phytase with thermostability increasing substitutions identified in directed evolution.Novel phytases from Bifidobacterium pseudocatenulatum ATCC 27919 and Bifidobacterium longum subsp. infantis ATCC 15697.Heterologous Expression of Secreted Bacterial BPP and HAP Phytases in Plants Stimulates Arabidopsis thaliana Growth on Phytate.Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications.Current Progresses in Phytase Research: Three-Dimensional Structure and Protein Engineering
P2860

Crystal structure of Klebsiella sp. ASR1 phytase suggests substrate binding to a preformed active site that meets the requirements of a plant rhizosphere enzyme

Item
http://www.wikidata.org/entity/Q27660528
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2010 nî lūn-bûn
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2010 թուականի Մարտին հրատարակուած գիտական յօդուած
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2010 թվականի մարտին հրատարակված գիտական հոդված
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2010年の論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年论文
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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Crystal structure of Klebsiell ...... of a plant rhizosphere enzyme
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10.1111/J.1742-4658.2010.07559.X
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P433
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