Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase. - Test2 - elhamkhani - TriplyDB

Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase.

Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase.

http://www.wikidata.org/entity/Q31060519

about

Identification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesign The quest for molecular quasi-species in ligand-activity space and its application to directed enzyme evolution.The evolution of catalytic efficiency and substrate promiscuity in human theta class 1-1 glutathione transferase.Drosophila GSTs display outstanding catalytic efficiencies with the environmental pollutants 2,4,6-trinitrotoluene and 2,4-dinitrotoluene.Cys-X scanning for expansion of active-site residues and modulation of catalytic functions in a glutathione transferase.Porcine glutathione transferase Alpha 2-2 is a human GST A3-3 analogue that catalyses steroid double-bond isomerization.Exploring sequence-function space of a poplar glutathione transferase using designed information-rich gene variants.

P2860

Q28217881-0D49CA62-FD48-4929-BE59-AB85CF94606B Q30981263-0DA3A700-232B-4ACF-88A1-70DDEC5D17B3 Q33258955-C7AC8869-7A89-4BC4-8F0D-42513069A0D7 Q41683384-203EA461-E6F4-446D-B280-E7AAAF964B92 Q42728408-0EABAF91-8EEF-4AC0-90DE-40F953A15CA7 Q42951273-4BD2D7F0-F904-464C-B06A-95D2F7BF6EAF Q47611061-C0DF2DB6-210B-4A64-A1A2-0A9ECB2993C4

P2860

Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase.

http://www.wikidata.org/entity/Q31060519

description

2002 nî lūn-bûn

@nan

2002 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Transmutation of human glutath ...... n efficient steroid isomerase.

@ast

Transmutation of human glutath ...... n efficient steroid isomerase.

@en

type

label

Transmutation of human glutath ...... n efficient steroid isomerase.

@ast

Transmutation of human glutath ...... n efficient steroid isomerase.

@en

prefLabel

Transmutation of human glutath ...... n efficient steroid isomerase.

@ast

Transmutation of human glutath ...... n efficient steroid isomerase.

@en

P1433

Q31060519-9ABBC17B-306F-4977-BA54-9DC354A18079

P1476

Q31060519-9FDC6727-9E7C-4CB6-B5E5-9EB815A0B708

P2093

Q31060519-04AD5079-8B20-4B67-9B4E-1068B84B261B

Q31060519-3BD7C4AB-679A-4E95-A4F7-463A0E5BFACF

Q31060519-CD02996F-A179-4504-BC7B-53804CC7A0E6

P2860

Q31060519-0BA1647F-A919-49A5-8483-50E127D2799F

Q31060519-1A35A3FA-5067-427D-9FAD-91EBAA967616

Q31060519-1A99A69A-9C72-4333-9A0C-7D2E95BDFD92

Q31060519-23B4F830-79E0-42A3-9E52-00DAB737C830

Q31060519-261CD2E0-5E06-4F36-8453-77B7DBD7C416

Q31060519-3A4B3470-7B65-4A42-8E36-970D749433B6

Q31060519-47CD00B7-3C44-4AC4-AD24-3255BB456047

Q31060519-57FA4088-4D85-409C-BA7C-337AEF6A50E6

Q31060519-6097144B-0B02-420B-B9FD-6937D3AB8E51

Q31060519-780F7C1C-F376-496F-8187-A7F2A407E4E0

P304

Q31060519-3FA61712-2EB5-416C-8E1E-E7ACBAB16409

P31

Q31060519-6EDB2650-1211-4345-B91B-36F6911A1610

P356

Q31060519-7108DC13-330B-4563-8B80-E0D382024239

P407

Q31060519-C25616A3-2B40-4857-BA86-0F178C249E6E

P433

Q31060519-E0473BF6-DD5A-4413-BBDB-41A4050B72D4

P478

Q31060519-FFE777E8-97AD-4D28-8EB7-D12F4052D068

P577

Q31060519-93062EA3-F714-4117-A9EB-BEDE12081A9E

P5875

Q31060519-353048CC-EA28-4FDC-BD41-E5D41A4DE267

P698

Q31060519-1ABF2455-D991-4DC7-9ED4-7CF4606F5509

P356

P1433

Journal of Biological Chemistry

P1476

Transmutation of human glutath ...... n efficient steroid isomerase.

@en

P2093

Ann-Sofie Johansson

http://www.w3.org/2001/XMLSchema#string

Bengt Mannervik

http://www.w3.org/2001/XMLSchema#string

Par L Pettersson

http://www.w3.org/2001/XMLSchema#string

P2860

Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes

Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate

Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues

Active-site residues governing high steroid isomerase activity in human glutathione transferase A3-3

Benzoic acid derivatives induce recovery of catalytic activity in the partially inactive Met208Lys mutant of human glutathione transferase A1-1

Human placental 3 beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5----4-ene-isomerase: purification from mitochondria and kinetic profiles, biophysical characterization of the purified mitochondrial and microsomal enzymes

Estimating the number of protein folds and families from complete genome data.

Computational method to reduce the search space for directed protein evolution.

Protein evolution by molecular breeding.

The role of human glutathione S-transferases hGSTA1-1 and hGSTA2-2 in protection against oxidative stress.

P304

30019-30022

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M204485200

http://www.w3.org/2001/XMLSchema#string

P407

P433

33

http://www.w3.org/2001/XMLSchema#string

P478

277

http://www.w3.org/2001/XMLSchema#string

P577

2002-05-21T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11349315

http://www.w3.org/2001/XMLSchema#string

P698

12023294

http://www.w3.org/2001/XMLSchema#string