A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site
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The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site lid conformations 1Structure and Metal Loading of a Soluble Periplasm CuproproteinA Structural Element That Facilitates Proton-Coupled Electron Transfer in Oxalate DecarboxylaseAssigning the EPR Fine Structure Parameters of the Mn(II) Centers in Bacillus subtilis Oxalate Decarboxylase by Site-Directed Mutagenesis and DFT/MM CalculationsStructural and functional insights into Saccharomyces cerevisiae Tpa1, a putative prolylhydroxylase influencing translation termination and transcription.Variations in Mn(II) speciation among organisms: what makes D. radiodurans different.Metal dependence of oxalate decarboxylase activity.Substrate Binding Mode and Molecular Basis of a Specificity Switch in Oxalate Decarboxylase.Kinetic and spectroscopic studies of bicupin oxalate oxidase and putative active site mutantsNitric oxide reversibly inhibits Bacillus subtilis oxalate decarboxylase.EPR spin trapping of an oxalate-derived free radical in the oxalate decarboxylase reaction.Protein similarity networks reveal relationships among sequence, structure, and function within the Cupin superfamily.Observation of superoxide production during catalysis of Bacillus subtilis oxalate decarboxylase at pH 4.Investigating the roles of putative active site residues in the oxalate decarboxylase from Bacillus subtilis.A previously unidentified sigma factor and two accessory proteins regulate oxalate decarboxylase expression in Bacillus subtilisOxygen activation by mononuclear Mn, Co, and Ni centers in biology and synthetic complexes.In vitro degradation of oxalate by recombinant Lactobacillus plantarum expressing heterologous oxalate decarboxylase.Cloning and sequencing of two Ceriporiopsis subvermispora bicupin oxalate oxidase allelic isoforms: implications for the reaction specificity of oxalate oxidases and decarboxylases.pH-dependent structures of the manganese binding sites in oxalate decarboxylase as revealed by high-field electron paramagnetic resonance.Secretion of biologically active heterologous oxalate decarboxylase (OxdC) in Lactobacillus plantarum WCFS1 using homologous signal peptides.Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.Recombinant oxalate decarboxylase: enhancement of a hybrid catalytic cascade for the complete electro-oxidation of glycerol.Oxalic acid production byFusarium oxysporumSchlecht andBotryodiplodia theobromaePat., post-harvest fungal pathogens of yams (Dioscorea rotundataL.) and detoxification byBacillus subtilisCM1 isolated from culturable cowdung microflora
P2860
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P2860
A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site
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2004 nî lūn-bûn
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2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2004 թվականի մայիսին հրատարակված գիտական հոդված
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2004年の論文
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2004年論文
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2004年論文
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2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
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name
A closed conformation of Bacil ...... ue identity of the active site
@ast
A closed conformation of Bacil ...... ue identity of the active site
@en
A closed conformation of Bacil ...... ue identity of the active site
@nl
type
label
A closed conformation of Bacil ...... ue identity of the active site
@ast
A closed conformation of Bacil ...... ue identity of the active site
@en
A closed conformation of Bacil ...... ue identity of the active site
@nl
prefLabel
A closed conformation of Bacil ...... ue identity of the active site
@ast
A closed conformation of Bacil ...... ue identity of the active site
@en
A closed conformation of Bacil ...... ue identity of the active site
@nl
P2093
P2860
P3181
P356
P1476
A closed conformation of Bacil ...... ue identity of the active site
@en
P2093
Adam Tanner
Clare E M Stevenson
David M Lawson
Laura Bowater
Stephen Bornemann
Victoria J Just
P2860
P304
P3181
P356
10.1074/JBC.M313820200
P407
P577
2004-05-07T00:00:00Z