Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase.
about
Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycleMalonate-bound structure of the glycerophosphodiesterase fromEnterobacter aerogenes(GpdQ) and characterization of the native Fe2+metal-ion preferenceSubstrate-Promoted Formation of a Catalytically Competent Binuclear Center and Regulation of Reactivity in a Glycerophosphodiesterase from Enterobacter aerogenesIdentification of purple acid phosphatase inhibitors by fragment-based screening: promising new leads for osteoporosis therapeuticsThe structure of a purple acid phosphatase involved in plant growth and pathogen defence exhibits a novel immunoglobulin-like foldA phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activityIdentification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases?Structural and enzymatic characterization of the streptococcal ATP/diadenosine polyphosphate and phosphodiester hydrolase Spr1479/SapH.Characterization of purple acid phosphatases involved in extracellular dNTP utilization in StylosanthesA molecular description of acid phosphatase.Spectroscopic and mechanistic studies of dinuclear metallohydrolases and their biomimetic complexes.Metallophosphoesterases: structural fidelity with functional promiscuity.Characterization of Wall Teichoic Acid Degradation by the Bacteriophage ϕ29 Appendage Protein GP12 Using Synthetic Substrate Analogs.The divalent metal ion in the active site of uteroferrin modulates substrate binding and catalysisCrystal structure of the Bacillus subtilis phosphodiesterase PhoD reveals an iron and calcium-containing active site.Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site.A complex iron-calcium cofactor catalyzing phosphotransfer chemistry.Mechanism of the phosphatase component of Clostridium thermocellum polynucleotide kinase-phosphatase.Theoretical studies on the reaction mechanism of PP1 and the effects of different oxidation states of the Mn-Mn center on the mechanism.Visualization of the Reaction Trajectory and Transition State in a Hydrolytic Reaction Catalyzed by a Metalloenzyme.Theoretical studies on the mechanism of activation of phosphoprotein phosphatases and purple acid phosphatases suggest an evolutionary strategy to survive in acidic environments.Triesterase and promiscuous diesterase activities of a di-Co(II)-containing organophosphate degrading enzyme reaction mechanisms.
P2860
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P2860
Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase.
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Phosphate forms an unusual tri ...... otato purple acid phosphatase.
@ast
Phosphate forms an unusual tri ...... otato purple acid phosphatase.
@en
type
label
Phosphate forms an unusual tri ...... otato purple acid phosphatase.
@ast
Phosphate forms an unusual tri ...... otato purple acid phosphatase.
@en
prefLabel
Phosphate forms an unusual tri ...... otato purple acid phosphatase.
@ast
Phosphate forms an unusual tri ...... otato purple acid phosphatase.
@en
P2093
P2860
P50
P356
P1476
Phosphate forms an unusual tri ...... potato purple acid phosphatase
@en
P2093
John de Jersey
Lawrence R Gahan
Lyle E Carrington
Mohsen Valizadeh
Susan E Hamilton
P2860
P304
P356
10.1073/PNAS.0407239102
P407
P577
2004-12-29T00:00:00Z