The FAD synthetase from the human pathogen Streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements.

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Discovery of antimicrobial compounds targeting bacterial type FAD synthetases.The RFK catalytic cycle of the pathogen Streptococcus pneumoniae shows species-specific features in prokaryotic FMN synthesis.

P2860

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P2860

The FAD synthetase from the human pathogen Streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements.

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http://www.wikidata.org/entity/Q40101380

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

@zh-my

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@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

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The FAD synthetase from the hu ...... -dependent redox requirements.

@en

type

Item

label

The FAD synthetase from the hu ...... -dependent redox requirements.

@en

prefLabel

The FAD synthetase from the hu ...... -dependent redox requirements.

@en

P1476

The FAD synthetase from the hu ...... y-dependent redox requirements

@en

P2093

Ana Serrano

http://www.w3.org/2001/XMLSchema#string

Erandi Lira-Navarrete

http://www.w3.org/2001/XMLSchema#string

María Sebastián

http://www.w3.org/2001/XMLSchema#string

P2860

Molecular characterization of mitochondrial apoptosis-inducing factor

Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch

Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes

Crystal structure of a flavin-binding protein from Thermotoga maritima

Structure and Mechanism of a Eukaryotic FMN Adenylyltransferase

Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase.

Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes

Key residues at the riboflavin kinase catalytic site of the bifunctional riboflavin kinase/FMN adenylyltransferase from Corynebacterium ammoniagenes

Quaternary organization in a bifunctional prokaryotic FAD synthetase: Involvement of an arginine at its adenylyltransferase module on the riboflavin kinase activity

Structural insights into the synthesis of FMN in prokaryotic organisms

P2888

s41598-017-07716-5

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scholarly article

P356

10.1038/S41598-017-07716-5

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Marta Martínez-Júlvez

Milagros Medina

Adrian Velazquez-campoy

Anabel Lostao

Ramón Hurtado-Guerrrero

C Marcuello

P577

2017-08-08T00:00:00Z

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P698

28790457

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P932

5548840

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The FAD synthetase from the human pathogen Streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements.

about

P2860

P2860

The FAD synthetase from the human pathogen Streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932