Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation.
about
Forced evolution of a herbicide detoxifying glutathione transferaseStructural Analysis of a Glutathione Transferase A1-1 Mutant Tailored for High Catalytic Efficiency with Toxic AlkenalsSubstrate Specificity Combined with Stereopromiscuity in Glutathione Transferase A4-4-Dependent Metabolism of 4-HydroxynonenalIdentification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesignContribution of aromatic-aromatic interactions to the anomalous pK(a) of tyrosine-9 and the C-terminal dynamics of glutathione S-transferase A1-1Zebra: a web server for bioinformatic analysis of diverse protein families.Cloning, expression and analysis of the olfactory glutathione S-transferases in coho salmon.The quest for molecular quasi-species in ligand-activity space and its application to directed enzyme evolution.Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase.Ensemble perspective for catalytic promiscuity: calorimetric analysis of the active site conformational landscape of a detoxification enzyme.Interactions of glutathione transferases with 4-hydroxynonenal.The anomalous pKa of Tyr-9 in glutathione S-transferase A1-1 catalyzes product release.Reengineering the glutathione S-transferase scaffold: a rational design strategy pays off.The stereochemical course of 4-hydroxy-2-nonenal metabolism by glutathione S-transferasesEnzymatic detoxication, conformational selection, and the role of molten globule active sites.The human hGSTA5 gene encodes an enzymatically active protein.Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1.Role of CRD-BP in the growth of human basal cell carcinoma cells.Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase.Drosophila GSTs display outstanding catalytic efficiencies with the environmental pollutants 2,4,6-trinitrotoluene and 2,4-dinitrotoluene.Reciprocal regulation of glutathione S-transferase spliceforms and the Drosophila c-Jun N-terminal kinase pathway componentsThe intersubunit lock-and-key motif in human glutathione transferase A1-1: role of the key residues Met51 and Phe52 in function and dimer stabilityCys-X scanning for expansion of active-site residues and modulation of catalytic functions in a glutathione transferase.Minor modifications of the C-terminal helix reschedule the favored chemical reactions catalyzed by theta class glutathione transferase T1-1.A conserved N-capping motif contributes significantly to the stabilization and dynamics of the C-terminal region of class Alpha glutathione S-transferases.Lifespan and stress resistance of Caenorhabditis elegans are increased by expression of glutathione transferases capable of metabolizing the lipid peroxidation product 4-hydroxynonenal.Exploring sequence-function space of a poplar glutathione transferase using designed information-rich gene variants.Functional promiscuity correlates with conformational heterogeneity in A-class glutathione S-transferases
P2860
Q27640970-AAB0D7A8-A963-47F7-A5C3-00085C186A52Q27646550-846A6C2A-A125-4F9F-A013-2F3793132257Q27659040-D0B6A3F5-620A-41A5-AA27-5077CA2954B7Q28217881-650C5C55-2290-4CB9-85FF-FCA7AC9A901FQ28346763-0EE9D54C-F894-437E-911B-320C4E684D9EQ30353542-B865600D-7E21-4CB1-81CE-FD63B1D97A9AQ30425057-06056563-0BA9-4741-B33D-61D04254EA44Q30981263-A35959D6-5394-450E-9CAA-50E97EDC1FE1Q31060519-6097144B-0B02-420B-B9FD-6937D3AB8E51Q35605100-241BB3D3-401F-4E22-AA04-35EF5E558C5DQ35731685-3FF8583F-D70C-4752-B0BA-EBC4DD640E9CQ35933692-25271BF2-0417-41C3-8B61-517068C8B79EQ36112285-4028B7F4-5BE6-4854-975E-8E365198730CQ36711101-FBA8B454-BCF4-41F2-9DC8-4E3CC11A66D9Q36947894-2E8354E8-D04B-4A59-83AB-A10ED2F61777Q37456829-C2215D8D-0232-4EFA-A108-503A213D3907Q37513208-38DBB143-1779-4389-B1B4-6A51D178967DQ39030031-97315949-9139-464A-81C0-CEFD4967D995Q41605240-EBBC2256-63C3-4709-AB19-9D3E4B81AB51Q41683384-FFCD38C8-F18F-4378-9D71-63F166F41501Q41825747-9E0C6CB6-EC25-400C-A267-9E47A9C16AD9Q41970895-CB75038D-D7BF-45AB-9D0D-C1B94F1D1982Q42728408-261FC9BF-54C7-435B-86A4-66A25F88CB5FQ42918008-8ADCEEB5-1652-438D-809E-F93AB8C82FAAQ46367673-7F68A9AC-1C17-4763-83A6-87DCFF871EFCQ46704667-38102FEC-8004-4C45-896C-B6A60DA9707EQ47611061-97D25F5A-3D0C-4FCD-BC41-128576FB09E6Q57447557-53362C98-2A51-4C72-B115-C3283EB39457
P2860
Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation.
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
name
Redesign of substrate-selectiv ...... roducts of lipid peroxidation.
@ast
Redesign of substrate-selectiv ...... roducts of lipid peroxidation.
@en
type
label
Redesign of substrate-selectiv ...... roducts of lipid peroxidation.
@ast
Redesign of substrate-selectiv ...... roducts of lipid peroxidation.
@en
prefLabel
Redesign of substrate-selectiv ...... roducts of lipid peroxidation.
@ast
Redesign of substrate-selectiv ...... roducts of lipid peroxidation.
@en
P2093
P2860
P356
P1476
Redesign of substrate-selectiv ...... roducts of lipid peroxidation.
@en
P2093
Gustafsson A
Mannervik B
Nilsson LO
P2860
P304
P356
10.1073/PNAS.150084897
P407
P577
2000-08-01T00:00:00Z