Characterization of phenylpyruvate decarboxylase, involved in auxin production of Azospirillum brasilense. - Wikidata - wikimedia - TriplyDB

Characterization of phenylpyruvate decarboxylase, involved in auxin production of Azospirillum brasilense.

Characterization of phenylpyruvate decarboxylase, involved in auxin production of Azospirillum brasilense.

http://www.wikidata.org/entity/Q42910224

about

Biological nitrogen fixation in non-legume plants Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae.Engineering Pseudomonas protegens Pf-5 for nitrogen fixation and its application to improve plant growth under nitrogen-deficient conditions Production of aromatic compounds by metabolically engineered Escherichia coli with an expanded shikimate pathway Plant growth-promoting rhizobacteria and root system functioning.Auxin and plant-microbe interactions.Symbiosis as a general principle in eukaryotic evolution.The ipdC, hisC1 and hisC2 genes involved in indole-3-acetic production used as alternative phylogenetic markers in Azospirillum brasilense.Exploring the Potentials of Lysinibacillus sphaericus ZA9 for Plant Growth Promotion and Biocontrol Activities against Phytopathogenic Fungi.Genome Sequence of Azospirillum brasilense CBG497 and Comparative Analyses of Azospirillum Core and Accessory Genomes provide Insight into Niche Adaptation Aromatic amino acid-dependent expression of indole-3-pyruvate decarboxylase is regulated by TyrR in Enterobacter cloacae UW5 Genetic analysis of the upper phenylacetate catabolic pathway in the production of tropodithietic acid by Phaeobacter gallaeciensis Analysis of genes contributing to plant-beneficial functions in Plant Growth-Promoting Rhizobacteria and related Proteobacteria Indole-3-butyric acid induces lateral root formation via peroxisome-derived indole-3-acetic acid and nitric oxide.Production of the Plant Hormone Auxin by Salmonella and Its Role in the Interactions with Plants and Animals.Auxin Biosynthesis: Are the Indole-3-Acetic Acid and Phenylacetic Acid Biosynthesis Pathways Mirror Images?Indole-3-acetaldehyde dehydrogenase-dependent auxin synthesis contributes to virulence of Pseudomonas syringae strain DC3000.The roles of auxin during interactions between bacterial plant pathogens and their hosts.Tryptophan, thiamine and indole-3-acetic acid exchange between Chlorella sorokiniana and the plant growth-promoting bacterium Azospirillum brasilense.Regulation of indole-3-acetic acid biosynthesis by branched-chain amino acids inEnterobacter cloacaeUW5 Control of the Cooperation Between Plant Growth-Promoting Rhizobacteria and Crops by Rhizosphere Signals

P2860

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P2860

Characterization of phenylpyruvate decarboxylase, involved in auxin production of Azospirillum brasilense.

http://www.wikidata.org/entity/Q42910224

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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name

Characterization of phenylpyru ...... on of Azospirillum brasilense.

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Characterization of phenylpyru ...... on of Azospirillum brasilense.

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type

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Characterization of phenylpyru ...... on of Azospirillum brasilense.

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Characterization of phenylpyru ...... on of Azospirillum brasilense.

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prefLabel

Characterization of phenylpyru ...... on of Azospirillum brasilense.

@en

Characterization of phenylpyru ...... on of Azospirillum brasilense.

@nl

P1433

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P1433

Journal of Bacteriology

P1476

Characterization of phenylpyru ...... on of Azospirillum brasilense.

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P2093

Jos Vanderleyden

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Martina Pohl

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Wim Versées

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P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

The structural basis of substrate activation in yeast pyruvate decarboxylase. A crystallographic and kinetic study

Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase

Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid

The crystal structure of phenylpyruvate decarboxylase from Azospirillum brasilense at 1.5 A resolution. Implications for its catalytic and regulatory mechanism

Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution

The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes

High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases

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7626-7633

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10.1128/JB.00830-07

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