Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
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Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymesThe Cellular Antiviral Protein Viperin Is Attenuated by Proteasome-Mediated Protein Degradation in Japanese Encephalitis Virus-Infected CellsCrystal Structure of the Heme d 1 Biosynthesis Enzyme NirE in Complex with Its Substrate Reveals New Insights into the Catalytic Mechanism of S -Adenosyl-l-methionine-dependent Uroporphyrinogen III MethyltransferasesOxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganeseLactococcus lactis HemW (HemN) is a haem-binding protein with a putative role in haem traffickingThe Pseudomonas aeruginosa nirE gene encodes the S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase required for heme d(1) biosynthesisEvolutionary Aspects and Regulation of Tetrapyrrole Biosynthesis in Cyanobacteria under Aerobic and Anaerobic EnvironmentsAerobic and anaerobic Mg-protoporphyrin monomethyl ester cyclases in purple bacteria: a strategy adopted to bypass the repressive oxygen control system.Stoichiometry of the redox neutral deamination and oxidative dehydrogenation reactions catalyzed by the radical SAM enzyme DesII.Analyses of MbtB, MbtE, and MbtF suggest revisions to the mycobactin biosynthesis pathway in Mycobacterium tuberculosis'Ca. Liberibacter asiaticus' proteins orthologous with pSymA-encoded proteins of Sinorhizobium meliloti: hypothetical roles in plant host interaction.Adenosyl radical: reagent and catalyst in enzyme reactions.Biochemical and Spectroscopic Characterization of a Radical S-Adenosyl-L-methionine Enzyme Involved in the Formation of a Peptide Thioether Cross-Link.The Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA PeptideDinucleotide spore photoproduct, a minimal substrate of the DNA repair spore photoproduct lyase enzyme from Bacillus subtilis.Mechanistic diversity of radical S-adenosylmethionine (SAM)-dependent methylation.Nfu facilitates the maturation of iron-sulfur proteins and participates in virulence in Staphylococcus aureus.Molecular clues to understand the aerotolerance phenotype of Bifidobacterium animalis subsp. lactisStructural and functional comparison of HemN to other radical SAM enzymes.Activation of cholera toxin production by anaerobic respiration of trimethylamine N-oxide in Vibrio choleraeChemical and Biological Reduction of the Radical SAM Enzyme 7-Carboxy-7-deazaguanine [corrected] Synthase.Controlling the delicate balance of tetrapyrrole biosynthesis.AdoMet radical proteins--from structure to evolution--alignment of divergent protein sequences reveals strong secondary structure element conservationRadical new paradigm for heme degradation in Escherichia coli O157:H7.Radical S-adenosylmethionine enzymes.Structure and function of enzymes in heme biosynthesis.Structural insights into radical generation by the radical SAM superfamily.Radical S-adenosylmethionine enzymes: mechanism, control and function.DNA Repair by the Radical SAM Enzyme Spore Photoproduct Lyase: From Biochemistry to Structural Investigations.Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Metabolic engineering of cobalamin (vitamin B12) production in Bacillus megateriumMechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis.Crystal structure of the oxygen-dependant coproporphyrinogen oxidase (Hem13p) of Saccharomyces cerevisiae.In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters.The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX.Posttranslational modification of serine to formylglycine in bacterial sulfatases. Recognition of the modification motif by the iron-sulfur protein AtsB.Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB.Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines.ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis.The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine.
P2860
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P2860
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
description
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2002
@ast
im September 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 13 September 2002)
@en
vedecký článok (publikovaný 2002/09/13)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/09/13)
@nl
наукова стаття, опублікована у вересні 2002
@uk
name
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@ast
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@en
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@nl
type
label
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@ast
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@en
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@nl
prefLabel
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@ast
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@en
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@nl
P2093
P2860
P356
P1476
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
@en
P2093
Esther Mahlitz
Gunhild Layer
Knut Verfürth
P2860
P304
34136-34142
P356
10.1074/JBC.M205247200
P407
P50
P577
2002-07-11T00:00:00Z