Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
about
How special is the biochemical function of native proteins?Structural and Enzymatic characterization of the lactonase SisLac from Sulfolobus islandicusCharacterisation of the organophosphate hydrolase catalytic activity of SsoPoxMolecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase TemplateHydrogen atoms in protein structures: high-resolution X-ray diffraction structure of the DFPaseDifferential active site loop conformations mediate promiscuous activities in the lactonase SsoPoxStructural and Enzymatic Characterization of the Phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenesSwitching a newly discovered lactonase into an efficient and thermostable phosphotriesterase by simple double mutations His250Ile/Ile263TrpParaoxonase 1 polymorphisms within a Mississippi USA population as possible biomarkers of enzyme activities associated with disease susceptibilityCrystallization and preliminary X-ray diffraction analysis of the lactonaseVmoLac fromVulcanisaeta moutnovskiaOn the role of physics and evolution in dictating protein structure and functionComputational protein engineering: bridging the gap between rational design and laboratory evolution.Paraoxonase 1 and homocysteine metabolism.Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis.Probing the mutational interplay between primary and promiscuous protein functions: a computational-experimental approachEnzyme promiscuity: engine of evolutionary innovation.Interplay of physics and evolution in the likely origin of protein biochemical functionExpanding the enzyme universe: accessing non-natural reactions by mechanism-guided directed evolution.Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily.Assessing the prediction fidelity of ancestral reconstruction by a library approach.Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro.Toward Understanding the Catalytic Mechanism of Human Paraoxonase 1: Site-Specific Mutagenesis at Position 192Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Specificity Effects of Amino Acid Substitutions in Promiscuous Hydrolases: Context-Dependence of Catalytic Residue Contributions to Local Fitness Landscapes in Nearby Sequence Space.Myeloperoxidase, paraoxonase-1, and HDL form a functional ternary complexCharacterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme.Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1.The Search for Dietary Supplements to Elevate or Activate Circulating Paraoxonases.Paraoxonase 1 in neurological disorders.The evolution of protein moonlighting: adaptive traps and promiscuity in the chaperonins.Quorum quenching: role in nature and applied developments.New chemiluminescent substrates of paraoxonase 1 with improved specificity: synthesis and properties.Modeling catalytic promiscuity in the alkaline phosphatase superfamily.Crystallization and preliminary X-ray diffraction analysis of the organophosphorus hydrolase OPHC2 from Pseudomonas pseudoalcaligenesNovel nucleophiles enhance the human serum paraoxonase 1 (PON1)-mediated detoxication of organophosphates.Molecular dynamics simulation of human serum paraoxonase 1 in DPPC bilayer reveals a critical role of transmembrane helix H1 for HDL association.Similar Active Sites and Mechanisms Do Not Lead to Cross-Promiscuity in Organophosphate Hydrolysis: Implications for Biotherapeutic Engineering.Structural plasticity mediates distinct GAP-dependent GTP hydrolysis mechanisms in Rab33 and Rab5.Assessment of the inhibitory effects and molecular docking of some sulfonamides on human serum paraoxonase 1.Towards Understanding the Catalytic Mechanism of Human Paraoxonase 1: Experimental and In Silico Mutagenesis Studies.
P2860
Q26766629-3998DFF3-2DCF-4226-975D-84D503E5002DQ27674600-FE4AE33B-B458-4CCA-8EDB-F612441FBB4BQ27675040-7C293220-456E-4F42-B070-8F29BB79E580Q27679003-ED403FC2-D9EB-4D10-9F9F-F3948D2D62C4Q27679371-7313D86F-CDB2-4911-A861-827179B4DB02Q27680130-4587345F-DA3A-44DC-8FC6-FDD7239E82B4Q27680592-91EA6425-A858-4EEC-9EB8-97FD879C439AQ27690108-D9F72BC9-2464-454E-9CFD-972D189CB8AAQ28243983-3F81BDE1-014B-425B-A9EE-9F6FACE2C452Q30047769-081EDA53-8D17-46CA-843A-215A3AEEE369Q30369480-3C645A16-2691-48D4-95D1-3FFFA33658B0Q30394571-AE9B6D8E-5618-493E-8C33-B237AE438175Q30417352-1E7EB817-EC9C-44E6-83DF-F54AC4FA855CQ30608426-B96C01FD-DCBA-4CF9-B917-F0EE1EC03F1EQ34311541-8F2891E0-0CE1-4C1E-A3A8-E0A6665AE67AQ34430867-7A9158D7-4E96-4622-AD88-935D26523ABAQ34729649-1BA6B569-1467-4679-91C8-2F3C8422FE65Q35504479-F2692F0C-849B-4DF8-9495-2DA57A58AD1AQ35669041-CE044EA3-09DA-4807-89B4-252C02976585Q35746785-565B9746-4875-4B24-B164-5207823D4797Q35854206-640B83DE-1F49-4871-913E-809293931DFEQ35909827-96370598-3991-4165-B446-0F506E974966Q36019839-A9C65E05-5D76-4698-84DA-AE97A18B5AFDQ36360999-FE716608-2C6C-4317-936B-F140A512281EQ37123887-8F58E8BC-E6F6-4F9F-A41B-D49D4155EF00Q37350343-95EFC97D-24D7-4F85-847F-24DA06904E99Q37609374-1B0ACFAD-4231-440F-95B2-2B085A502F2CQ37690989-9F6D4270-812E-4A52-9620-D88B78257F35Q38162323-91AC2973-4EE6-4821-B294-6D6BA95A4713Q38268475-6525EBBA-E765-4445-BAF6-EB5C7FD7A41FQ38598251-78EB301A-6678-4C58-BC22-37B7B6017DCFQ41158626-78182914-812D-4B1B-9215-6CE67B0B4289Q42024162-1DE89726-4A21-4BDB-AB01-B54247F8A250Q42096211-5BF6E467-ECD2-409D-8F34-E80703CB81EEQ42703917-E9CE1466-2173-455B-810B-992F7F004FC0Q45224671-FE68CFCE-53E7-45A3-94C9-F88F2E0D2E46Q47160816-69685A31-CFE4-406D-8090-4E5C543D86B1Q47449875-DB5ED36A-026A-4BD8-BB2A-FDECD9F5C3E9Q48194500-679FC750-9AE8-4D2B-8896-4AA940EB860EQ51017237-C6E2B6A2-DAFD-4591-B8CE-16EB5605D6B8
P2860
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@ast
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@en
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@nl
type
label
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@ast
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@en
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@nl
prefLabel
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@ast
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@en
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@nl
P2093
P50
P3181
P1476
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
@en
P2093
Dan S Tawfik
Elisabet Duñach
Jean-Jacques Filippi
Moshe Ben-David
P304
P3181
P356
10.1016/J.JMB.2012.02.042
P407
P577
2012-05-04T00:00:00Z