Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC - Test2 - elhamkhani - TriplyDB

Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

http://www.wikidata.org/entity/Q27648208

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Structure and Ligand Binding Properties of the Epoxidase Component of Styrene Monooxygenase,The FAD Cofactor of RebC Shifts to an IN Conformation upon Flavin Reduction † , ‡Structure of the PLP Degradative Enzyme 2-Methyl-3-hydroxypyridine-5-carboxylic Acid Oxygenase from Mesorhizobium loti MAFF303099 and Its Mechanistic Implications Crystal Structure of Baeyer−Villiger Monooxygenase MtmOIV, the Key Enzyme of the Mithramycin Biosynthetic Pathway,Insights into Substrate Specificity of Geranylgeranyl Reductases Revealed by the Structure of Digeranylgeranylglycerophospholipid Reductase, an Essential Enzyme in the Biosynthesis of Archaeal Membrane Lipids An Unusual Role for a Mobile Flavin in StaC-like Indolocarbazole Biosynthetic Enzymes Crystal Structure of 3-Hydroxybenzoate 6-Hydroxylase Uncovers Lipid-assisted Flavoprotein Strategy for Regioselective Aromatic Hydroxylation Divergent pathways in the biosynthesis of bisindole natural products.Total (bio)synthesis: strategies of nature and of chemists.Characterization of an environmental DNA-derived gene cluster that encodes the bisindolylmaleimide methylarcyriarubin Crystallography gets the jump on the enzymologists Form follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.Insights into Complex Oxidation during BE-7585A Biosynthesis: Structural Determination and Analysis of the Polyketide Monooxygenase BexE.Biosynthesis of indolocarbazole and goadsporin, two different heterocyclic antibiotics produced by actinomycetes.The biocatalytic repertoire of natural biaryl formation.Biosynthesis of nitrogen-containing natural products, C7N aminocyclitols and bis-indoles, from actinomycetes.Identification and characterization of a biosynthetic gene cluster for tryptophan dimers in deep sea-derived Streptomyces sp. SCSIO 03032.Structures of the Apo and FAD-bound forms of 2-hydroxybiphenyl 3-monooxygenase (HbpA) locate activity hotspots identified by using directed evolution.Regiodivergent N-C and N-N aryl coupling reactions of indoloterpenes and cycloether formation mediated by a single bacterial flavoenzyme.Rebeccamycin and staurosporine biosynthesis: insight into the mechanisms of the flavin-dependent monooxygenases RebC and StaC.

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P2860

Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

http://www.wikidata.org/entity/Q27648208

description

2007 nî lūn-bûn

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2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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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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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

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Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

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Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

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type

label

Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

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Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

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Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

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prefLabel

Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

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Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

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Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

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PNAS.0707190104

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC

@en

P2093

Annaleise R Howard-Jones

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Catherine L Drennan

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Christopher T Walsh

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Katherine S Ryan

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Michael J Hamill

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P2860

Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis

Combinatorial biosynthesis of antitumor indolocarbazole compounds

Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase

High-resolution structure of phenol hydroxylase and correction of sequence errors

The mobile flavin of 4-OH benzoate hydroxylase

The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis

Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum

Catalytic function of tyrosine residues in para-hydroxybenzoate hydroxylase as determined by the study of site-directed mutants

Thioredoxin--a fold for all reasons

Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.

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15311-15316

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scholarly article

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10.1073/PNAS.0707190104

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39

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104

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Sean J. Elliott

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2007-09-14T00:00:00Z

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5969927

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17873060

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2000502

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