IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli
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Biosynthesis and functions of sulfur modifications in tRNAStructural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein InteractionsA novel target of IscS in Escherichia coli: participating in DNA phosphorothioationFerredoxin competes with bacterial frataxin in binding to the desulfurase IscS.The mononuclear molybdenum enzymes.Elucidation of the dual role of Mycobacterial MoeZR in molybdenum cofactor biosynthesis and cysteine biosynthesis.The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli.Proteomic analysis of protein-protein interactions within the Cysteine Sulfinate Desulfinase Fe-S cluster biogenesis system.The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesisTransposon mutagenesis identified chromosomal and plasmid genes essential for adaptation of the marine bacterium Dinoroseobacter shibae to anaerobic conditions.Cleavage of the moaX-encoded fused molybdopterin synthase from Mycobacterium tuberculosis is necessary for activity.Deletion of the Proposed Iron Chaperones IscA/SufA Results in Accumulation of a Red Intermediate Cysteine Desulfurase IscS in Escherichia coli.Posttranslational modification of cellular proteins by a ubiquitin-like protein in bacteria.Biosynthesis of 4-thiouridine in tRNA in the methanogenic archaeon Methanococcus maripaludis.Metamorphic protein IscU changes conformation by cis-trans isomerizations of two peptidyl-prolyl peptide bonds.TusA (YhhP) and IscS are required for molybdenum cofactor-dependent base-analog detoxification.Archaeal proteasomes and sampylation.Global identification of genes affecting iron-sulfur cluster biogenesis and iron homeostasis.Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors.The biosynthesis of the molybdenum cofactors.Bacterial molybdoenzymes: old enzymes for new purposes.Post-translational thioamidation of methyl-coenzyme M reductase, a key enzyme in methanogenic and methanotrophic Archaea.A sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli.The iron-binding CyaY and IscX proteins assist the ISC-catalyzed Fe-S biogenesis in Escherichia coli.Discovery of piperonal-converting oxidase involved in the metabolism of a botanical aromatic aldehyde.Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly.The History of the Discovery of the Molybdenum Cofactor and Novel Aspects of its Biosynthesis in BacteriaCysteine desulphurase plays an important role in environmental adaptation of the hyperthermophilic archaeon Thermococcus kodakarensis.
P2860
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P2860
IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli
description
2009 nî lūn-bûn
@nan
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
IscS functions as a primary su ...... ybdopterin in Escherichia coli
@ast
IscS functions as a primary su ...... ybdopterin in Escherichia coli
@en
type
label
IscS functions as a primary su ...... ybdopterin in Escherichia coli
@ast
IscS functions as a primary su ...... ybdopterin in Escherichia coli
@en
prefLabel
IscS functions as a primary su ...... ybdopterin in Escherichia coli
@ast
IscS functions as a primary su ...... ybdopterin in Escherichia coli
@en
P2093
P2860
P356
P1476
IscS functions as a primary su ...... ybdopterin in Escherichia coli
@en
P2093
Alexander Urban
Hisaaki Mihara
Nobuyoshi Esaki
Tatsuo Kurihara
Wanjiao Zhang
P2860
P304
P356
10.1074/JBC.M109.082172
P407
P577
2009-11-29T00:00:00Z