Discovery of acetylene hydratase activity of the iron–sulphur protein IspH

Discovery of acetylene hydratase activity of the iron–sulphur protein IspH

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http://www.wikidata.org/entity/Q27671864
Structures of Fluoro, Amino, and Thiol Inhibitors Bound to the [Fe4S4] Protein IspHInsights into the Binding of Pyridines to the Iron–Sulfur Enzyme IspHUnsaturated C3,5,7,9-Monocarboxylic Acids by Aqueous, One-Pot Carbon Fixation: Possible Relevance for the Origin of LifeIsoprenoid Biosynthesis in Pathogenic Bacteria: Nuclear Resonance Vibrational Spectroscopy Provides Insight into the Unusual [4Fe-4S] Cluster of the E. coli LytB/IspH Protein.Bioorganometallic chemistry with IspG and IspH: structure, function, and inhibition of the [Fe(4)S(4)] proteins involved in isoprenoid biosynthesis.Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM)N-Terminal Region of GbIspH1, Ginkgo biloba IspH Type 1, May Be Involved in the pH-Dependent Regulation of Enzyme ActivityProteome scale comparative modeling for conserved drug and vaccine targets identification in Corynebacterium pseudotuberculosisAtomic-Resolution Structures of Discrete Stages on the Reaction Coordinate of the [Fe4S4] Enzyme IspG (GcpE)LytB1 and LytB2 of Mycobacterium tuberculosis Are Not Genetically RedundantMechanistic aspects of carotenoid biosynthesis.Exploring the Catalytic Promiscuity of Phenolic Acid Decarboxylases: Asymmetric, 1,6-Conjugate Addition of Nucleophiles Across 4-Hydroxystyrene.Mechanistic insights into the reductive dehydroxylation pathway for the biosynthesis of isoprenoids promoted by the IspH enzyme.Two unexpected promiscuous activities of the iron-sulfur protein IspH in production of isoprene and isoamylene.Spectroscopic and Computational Investigations of Ligand Binding to IspH: Discovery of Non-diphosphate Inhibitors.Further Insight into Crystal Structures of Escherichia coli IspH/LytB in Complex with Two Potent Inhibitors of the MEP Pathway: A Starting Point for Rational Design of New Antimicrobials.Functional evidence for the critical amino-terminal conserved domain and key amino acids of Arabidopsis 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE.
P2860

Discovery of acetylene hydratase activity of the iron–sulphur protein IspH

Item
http://www.wikidata.org/entity/Q27671864
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2012 nî lūn-bûn
@nan
2012 թուականին հրատարակուած գիտական յօդուած
@hyw
2012 թվականին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@ast
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@en
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@nl
type
label
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@ast
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@en
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@nl
prefLabel
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@ast
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@en
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@nl
P1433
P1476
P2093
P2860
P2888
P304
P31
P3181
P356
P407
P478
P50
P577
P6179
P698
P932
P3181
P356
P1433
P1476
Discovery of acetylene hydratase activity of the iron–sulphur protein IspH
@en
P2093
P2860
P2888
P304
P31
P3181
P356
P407
P478
P50
P577
P6179
P698
P932