A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase. - Wikidata - awgldk - TriplyDB

A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.

A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.

http://www.wikidata.org/entity/Q27648381

about

Erythroid heme biosynthesis and its disorders Porphyrin Binding and Distortion and Substrate Specificity in the Ferrochelatase Reaction: The Role of Active Site Residues Product Release Rather than Chelation Determines Metal Specificity for Ferrochelatase Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization A Novel Role for Progesterone Receptor Membrane Component 1 (PGRMC1): A Partner and Regulator of Ferrochelatase Identification and characterization of an inhibitory metal ion-binding site in ferrochelatase Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis Identification of the Mitochondrial Heme Metabolism Complex.Identification of a bacteria-like ferrochelatase in Strongyloides venezuelensis, an animal parasitic nematode.Nickel(II) chelatase variants directly evolved from murine ferrochelatase: porphyrin distortion and kinetic mechanism.Metal ion substrate inhibition of ferrochelatase.Resonance Raman Spectroscopic Examination of Ferrochelatase-induced Porphyrin Distortion.FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYS HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme synthesis in Firmicutes and Actinobacteria.One ring to rule them all: trafficking of heme and heme synthesis intermediates in the metazoans Identification and characterization of solvent-filled channels in human ferrochelatase.Structure and function of enzymes in heme biosynthesis.A conserved amphipathic ligand binding region influences k-path-dependent activity of cytochrome C oxidase.Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Dissecting π-helices: sequence, structure and function.Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase.Membrane-traversing mechanism of thyroid hormone transport by monocarboxylate transporter 8.Ferrochelatase π-helix: Implications from examining the role of the conserved π-helix glutamates in porphyrin metalation and product release.

P2860

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P2860

A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.

http://www.wikidata.org/entity/Q27648381

description

2007 nî lūn-bûn

@nan

2007 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2007年の論文

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2007年論文

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2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

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name

A pi-helix switch selective fo ...... lease in human ferrochelatase.

@ast

A pi-helix switch selective fo ...... lease in human ferrochelatase.

@en

A π-Helix Switch Selective for ...... elease in Human Ferrochelatase

@nl

type

label

A pi-helix switch selective fo ...... lease in human ferrochelatase.

@ast

A pi-helix switch selective fo ...... lease in human ferrochelatase.

@en

A π-Helix Switch Selective for ...... elease in Human Ferrochelatase

@nl

prefLabel

A pi-helix switch selective fo ...... lease in human ferrochelatase.

@ast

A pi-helix switch selective fo ...... lease in human ferrochelatase.

@en

A π-Helix Switch Selective for ...... elease in Human Ferrochelatase

@nl

P1433

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P356

J.JMB.2007.08.040

P1433

Journal of Molecular Biology

P1476

A pi-helix switch selective fo ...... elease in human ferrochelatase

@en

P2093

Harry A Dailey

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

Tamara A Dailey

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

Teresa A Ross

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

William N Lanzilotta

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P2860

Chelatases: distort to select?

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structural and mechanistic basis of porphyrin metallation by ferrochelatase

The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

Metal binding to Saccharomyces cerevisiae ferrochelatase

Metal binding to Bacillus subtilis ferrochelatase and interaction between metal sites

Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX

Substrate interactions with human ferrochelatase

Altered Orientation of Active Site Residues in Variants of Human Ferrochelatase. Evidence for a Hydrogen Bond Network Involved in Catalysis †

Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis

P304

1006-1016

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scholarly article

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10.1016/J.JMB.2007.08.040

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4

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P478

373

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5959267

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17884090

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P932

2083577

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