p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol (Q32081394)

6 July 2017

p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol (English)

1 reference

6 July 2017

Clostridium difficile

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author name string

T Selmer

series ordinal

1

1 reference

PubMed ID

11231288

6 July 2017

P I Andrei

series ordinal

2

1 reference

PubMed ID

11231288

6 July 2017

language of work or name

English

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publication date

1 March 2001

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6 July 2017

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6 July 2017

268

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6 July 2017

1363-1372

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6 July 2017

5

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Clinical impact and associated costs of Clostridium difficile-associated disease.

6 July 2017

1 reference

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Pathogenesis of Clostridium difficile infection.

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Effect of phenolic antioxidants on microbial growth

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Tolumonas auensis gen. nov., sp. nov., a toluene-producing bacterium from anoxic sediments of a freshwater lake

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p-Cresol formation by cell-free extracts of Clostridium difficile

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1 reference

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Unusual dehydrations in anaerobic bacteria: considering ketyls (radical anions) as reactive intermediates in enzymatic reactions

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Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis

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A new multiphasic buffer system for sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins and peptides with molecular masses 100,000-1000, and their detection with picomolar sensitivity

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The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri

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

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The complete genome sequence of Escherichia coli K-12

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The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus

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Post-translational activation introduces a free radical into pyruvate formate-lyase

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The free radical in pyruvate formate-lyase is located on glycine-734

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Ribonucleotide reductases

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Glycyl radical enzymes: a conservative structural basis for radicals

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Biochemical and genetic characterization of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism.

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Anaerobic toluene-catabolic pathway in denitrifying Thauera aromatica: activation and beta-oxidation of the first intermediate, (R)-(+)-benzylsuccinate

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Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase

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Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase

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Molecular properties of pyruvate formate-lyase activating enzyme.

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Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate

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Bacteriophage T4 anaerobic ribonucleotide reductase contains a stable glycyl radical at position 580.

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Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction.

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Bacterial Dissimilation of Indoleacetic Acid: a New Route of Breakdown of the Indole Nucleus

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Pyruvate Formate-Lyase-Activating Enzyme: Strictly Anaerobic Isolation Yields Active Enzyme Containing a [3Fe–4S]+ Cluster

21 January 2018

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21 January 2018

Identifiers

DOI

1 reference

6 July 2017

1 reference

PubMed ID

11231288