Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese.
about
The Impact of Non-Enzymatic Reactions and Enzyme Promiscuity on Cellular Metabolism during (Oxidative) Stress ConditionsThe RNA world and the origin of metabolic enzymesManganese homeostasis and utilization in pathogenic bacteriaThe widespread role of non-enzymatic reactions in cellular metabolismBattles with iron: manganese in oxidative stress protectionConditional iron and pH-dependent activity of a non-enzymatic glycolysis and pentose phosphate pathwayThe catalase activity of diiron adenine deaminaseA Molecular Mechanism for Bacterial Susceptibility to ZincImperfect coordination chemistry facilitates metal ion release in the Psa permeaseIntracellular hydrogen peroxide and superoxide poison 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase, the first committed enzyme in the aromatic biosynthetic pathway of Escherichia coli.The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacteriumNon-enzymatic glycolysis and pentose phosphate pathway-like reactions in a plausible Archean ocean.The relationship of the lipoprotein SsaB, manganese and superoxide dismutase in Streptococcus sanguinis virulence for endocarditis.The ins and outs of bacterial iron metabolism.Identifying neighborhoods of coordinated gene expression and metabolite profiles.The Escherichia coli MntR miniregulon includes genes encoding a small protein and an efflux pump required for manganese homeostasisNutritional immunity: transition metals at the pathogen-host interface.The mismetallation of enzymes during oxidative stress.The Escherichia coli small protein MntS and exporter MntP optimize the intracellular concentration of manganese.Dysregulation of IRP1-mediated iron metabolism causes gamma ray-specific radioresistance in leukemia cellsMetal limitation and toxicity at the interface between host and pathogenManganese (Mn) oxidation increases intracellular Mn in Pseudomonas putida GB-1.The YaaA protein of the Escherichia coli OxyR regulon lessens hydrogen peroxide toxicity by diminishing the amount of intracellular unincorporated iron.Extracellular zinc competitively inhibits manganese uptake and compromises oxidative stress management in Streptococcus pneumoniae.Diagnosing oxidative stress in bacteria: not as easy as you might thinkGeneral and condition-specific essential functions of Pseudomonas aeruginosa.The induction of two biosynthetic enzymes helps Escherichia coli sustain heme synthesis and activate catalase during hydrogen peroxide stress.Host-imposed manganese starvation of invading pathogens: two routes to the same destination.Regulation of manganese antioxidants by nutrient sensing pathways in Saccharomyces cerevisiaeManganese homeostasis in group A Streptococcus is critical for resistance to oxidative stress and virulence.The Staphylococcus aureus ABC-Type Manganese Transporter MntABC Is Critical for Reinitiation of Bacterial Replication Following Exposure to Phagocytic Oxidative BurstNramp1 and Other Transporters Involved in Metal Withholding during Infection.Mononuclear iron enzymes are primary targets of hydrogen peroxide stressWhy do bacteria use so many enzymes to scavenge hydrogen peroxide?Transcription Factors That Defend Bacteria Against Reactive Oxygen SpeciesA Matter of Timing: Contrasting Effects of Hydrogen Sulfide on Oxidative Stress Response in Shewanella oneidensis.Systematic engineering of pentose phosphate pathway improves Escherichia coli succinate production.A Superoxide Dismutase Capable of Functioning with Iron or Manganese Promotes the Resistance of Staphylococcus aureus to Calprotectin and Nutritional Immunity.Peroxide-sensing transcriptional regulators in bacteriaStructure, kinetic characterization and subcellular localization of the two ribulose 5-phosphate epimerase isoenzymes from Trypanosoma cruzi
P2860
Q26785889-C1F1EA70-3ED8-4AA9-959F-8373F13BEE20Q26852111-391D7534-A60F-4F92-AB17-A7AB0204BD61Q26852442-590D4CC4-E788-4A58-854F-8AC219CA5481Q26996495-42B79F3E-3F6E-4798-AEA3-53E8A12410EDQ27025367-FA5EEDA3-5FFC-4936-9C3C-0C89F0A52842Q27335088-10857965-D849-4737-B624-3F3777600DB8Q27675029-3F8D0D82-3FE4-4AD6-9BFA-087F4C0D06C0Q27675498-206CEFFD-3F63-4C64-B8CC-358E580E670CQ27687486-B73C3862-6C33-4C48-B8C1-1582985F8C19Q33570133-D3DDD078-B314-446B-AAD0-83D4071BB5E0Q33601261-1A8F9DF7-F02D-4B20-B394-9AB6F56BB2D6Q33621532-44F58D73-C290-4E41-AC82-E625A6BE97AEQ33803177-C55AA35A-6D4E-4450-81E8-7BE1E57ED564Q34055559-24CBBE96-0549-41B7-9051-96D38EBC43D5Q34166321-802CBD9D-931E-411F-A86C-A87F1AD0BB34Q34215344-629A5969-42DF-47A4-8683-2D910C7C59AFQ34288184-8CA57F0B-120B-4070-BAEF-4C88A0938C25Q34317281-9BB1F87F-C12D-4025-BAB0-004E0B539898Q34467289-B7D166CE-FC19-49D5-ACE3-EFFE8CE350BEQ34479123-1001E341-5238-4629-B6F7-880CFFE06548Q34490463-75DCDF6A-F8A6-4A44-9BF3-D483AD882019Q35023458-BC49CE95-BBEC-477C-BBA4-046BF6D2B68EQ35095921-BB4BC423-B083-4686-8069-87D8BA38524BQ35099868-BD2060DE-3BBE-427A-B1C5-38BB51079292Q35235708-5D37C0EF-4E32-4C75-B7FB-14951916612FQ35549350-A811FFD5-12D0-447C-948E-55844AD928ACQ35602469-8CB3A13C-D481-47EB-B8C4-0EE62919853FQ35602649-B532C7ED-801B-4AD5-8A34-EB39E4B1B6CAQ35620390-EC9B07CD-DE3C-41AA-82C1-0FCA255B2947Q35677580-C4DAEFEB-B580-403B-A770-7A0212FC7BC6Q35778485-2C9ACE0D-73FF-4DF5-B766-470A07BC65EEQ35905314-E327EADB-FEE6-4072-A2FB-E2E1A28B38C6Q35939868-8FCE6860-E9D6-4792-9559-1B90F2DE7A03Q36147012-F5822CD5-3659-44B2-8450-2194AEBF0F6AQ36199932-5CF77B58-F417-42DF-B8B9-D265C10797F8Q36208042-D23CA068-02F3-457E-9BFD-7805EDAB3DD3Q36226181-AC24E4ED-13F7-4A17-8DAE-74C2D4197CA9Q36254095-F0F6A6A5-9335-4B02-8726-D44B84FB9A82Q36281008-7E5CF49D-9200-4459-B824-1F696A8E716DQ36282777-A1B8D076-0721-426F-BD9A-978044775B4D
P2860
Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@ast
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@en
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@nl
type
label
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@ast
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@en
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@nl
prefLabel
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@ast
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@en
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@nl
P2860
P356
P1476
Iron enzyme ribulose-5-phospha ...... can be protected by manganese.
@en
P2093
James A Imlay
Jason M Sobota
P2860
P304
P356
10.1073/PNAS.1100410108
P407
P577
2011-03-14T00:00:00Z