Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity - Wikidata - awgldk - TriplyDB

Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity

Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity

http://www.wikidata.org/entity/Q24648730

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Evolutionary Aspects and Regulation of Tetrapyrrole Biosynthesis in Cyanobacteria under Aerobic and Anaerobic Environments Heme pathway evolution in kinetoplastid protists Mutations in hemG mediate resistance to salicylidene acylhydrazides, demonstrating a novel link between protoporphyrinogen oxidase (HemG) and Chlamydia trachomatis infectivity.The chlorite dismutase (HemQ) from Staphylococcus aureus has a redox-sensitive heme and is associated with the small colony variant phenotype.Heme biosynthesis is coupled to electron transport chains for energy generation.Discovery and Characterization of HemQ: an essential heme biosynthetic pathway component.Identification of a gene essential for protoporphyrinogen IX oxidase activity in the cyanobacterium Synechocystis sp. PCC6803.Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.Molecular phylogeny and intricate evolutionary history of the three isofunctional enzymes involved in the oxidation of protoporphyrinogen IX.Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin.Discovery of a gene involved in a third bacterial protoporphyrinogen oxidase activity through comparative genomic analysis and functional complementation.HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme synthesis in Firmicutes and Actinobacteria.Tetrapyrrole Metabolism in Arabidopsis thaliana.Characterization of Myxococcus xanthus MazF and implications for a new point of regulation.Structure and function of enzymes in heme biosynthesis.Recent advances in bacterial heme protein biochemistry.Recent advances in the biosynthesis of modified tetrapyrroles: the discovery of an alternative pathway for the formation of heme and heme d 1.Heme Synthesis and Acquisition in Bacterial Pathogens.Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.The Complex Transcriptional Response of Acaryochloris marina to Different Oxygen Levels Leishmania major possesses a unique HemG-type protoporphyrinogen IX oxidase.

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P2860

Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity

http://www.wikidata.org/entity/Q24648730

description

2009 nî lūn-bûn

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2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2009 թվականի հուլիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Identification of Escherichia ...... porphyrinogen oxidase activity

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Identification of Escherichia ...... porphyrinogen oxidase activity

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Identification of Escherichia ...... porphyrinogen oxidase activity

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Identification of Escherichia ...... porphyrinogen oxidase activity

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Identification of Escherichia ...... porphyrinogen oxidase activity

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Identification of Escherichia ...... porphyrinogen oxidase activity

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Identification of Escherichia ...... porphyrinogen oxidase activity

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Identification of Escherichia ...... porphyrinogen oxidase activity

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Harry A Dailey

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

Lauren E Daugherty

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

Tamara A Dailey

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

Tye O Boynton

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P2860

Rev-erbalpha, a heme sensor that coordinates metabolic and circadian pathways

Identification of heme as the ligand for the orphan nuclear receptors REV-ERBalpha and REV-ERBbeta.

Human protoporphyrinogen oxidase: expression, purification, and characterization of the cloned enzyme

Crystal Structure of the NADH:Quinone Oxidoreductase WrbA from Escherichia coli

Structural Insight into the Heme-based Redox Sensing by DosS from Mycobacterium tuberculosis

Expression of a cloned protoporphyrinogen oxidase

Heme-dependent up-regulation of the alpha-globin gene expression by transcriptional repressor Bach1 in erythroid cells

WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase

The Jpred 3 secondary structure prediction server

Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins.

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scholarly article

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1556297

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10.1021/BI900850Y

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29

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48

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2009-07-28T00:00:00Z

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26652914

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19583219

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P921

protoporphyrinogen oxidase activity

menaquinone-dependent protoporphyrinogen oxidase activity

Escherichia coli

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2749469

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