About: Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme

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About: Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme Goto Sponge NotDistinct Permalink

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scientific article published on 01 March 2000

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) wüsseschaftlicher Artikel, wo im März 2000 veröffentlicht worden isch (gsw) im März 2000 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в березні 2000 (uk) artículu científicu espublizáu en marzu de 2000 (ast) scientific article published on 01 March 2000 (en)
publication date	wds:Q73561096-EEC5E0C3-4CA3-404C-AF2A-024D5658CBB0
publication date	2000-03-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73561096-D016CE33-96A1-4A08-9A93-D795D4606BB0
language of work or name	English
cites work	wds:Q73561096-07B5A5C5-7732-4291-80D9-1B5ACD2107DB wds:Q73561096-0A4701EE-D98D-42CB-892B-9E51B91CEDF7 wds:Q73561096-12BF6E10-685D-456E-8FE6-C5E88981721B wds:Q73561096-12E59E47-D7E8-4855-AF42-2AD4151C184A wds:Q73561096-13C7560E-FAC0-4CDE-9231-D8331B9D4D50 wds:Q73561096-188C087D-516B-4D2B-B776-A33329D0484A wds:Q73561096-1919F8E4-3BA6-4B9D-96E1-F49A5580109F wds:Q73561096-22AADE3E-53A0-49D9-B3E6-C108C203B4B9 wds:Q73561096-3D05A987-A400-4EC9-92E8-EFDA294C8F69 wds:Q73561096-5B581B4E-D688-4E69-BB33-3DDA2CA2170C wds:Q73561096-61C78441-7C3A-4299-8A27-8815614293F2 wds:Q73561096-692E6CCF-43B1-4D0A-BC75-7F28EF8F6E7C wds:Q73561096-7CCC0168-A3E4-455E-B978-6BC38C25B4AD wds:Q73561096-8C25CE4D-AA32-45E5-BC06-072EB4A073DD wds:Q73561096-92CE99AA-E111-47C4-8688-38277CDB9DE4 wds:Q73561096-9B378B14-FCD7-4E65-B478-E16335039EF4 wds:Q73561096-9F31B9E3-25EC-4CE9-9C65-7478DE10D4AA wds:Q73561096-B89DD31C-F5B6-4F45-8CA8-3343E465631E wds:Q73561096-CDB70F32-95DD-44C4-983E-05EA8CDBF909 wds:Q73561096-DDB116B9-51F8-40E5-9BD4-016C537D04A4 wds:Q73561096-ED4E035A-0906-47B9-84F4-88606DF8C22C
cites work	Design of two chimaeric human-rat class alpha glutathione transferases for probing the contribution of C-terminal segments of protein structure to the catalytic properties Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding. Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative Fast product formation and slow product release are important features in a hysteretic reaction mechanism of glutathione transferase T2-2 Inhibition of glyoxalase I by S-substituted glutathiones Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site Theta, a new class of glutathione transferases purified from rat and man Structure, catalytic mechanism, and evolution of the glutathione transferases The reaction of aralkyl sulphate esters with glutathione catalysed by rat liver preparations Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties Kinetic independence of the subunits of cytosolic glutathione transferase from the rat. Enzymes harboring unnatural amino acids: mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface Benzoic acid derivatives induce recovery of catalytic activity in the partially inactive Met208Lys mutant of human glutathione transferase A1-1 Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues Biochemical studies of toxic agents. The metabolic formation of 1- and 2-menaphthylmercapturic acid Formation of mercapturic acids in rats after the administration of aralkyl esters Heterologous expression, purification and characterization of rat class theta glutathione transferase T2-2
author name string	wds:Q73561096-32434E65-2DE2-4E99-8DEA-C749A607E10C wds:Q73561096-EA73A1C0-CD34-4593-841A-5A598FF7A53A
author name string	B Mannervik P Jemth
rdfs:label	Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme (en) Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme (nl)
skos:prefLabel	Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme (en) Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme (nl)
name	Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme (en) Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme (nl)
title	wds:Q73561096-EA687463-2A58-4A9D-9298-1D9B3241CFB1
title	Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme (en)
page(s)	wds:Q73561096-237A4321-7AB4-4A69-9835-B8F66AF63C90
page(s)	8618-8624
instance of	wds:Q73561096-402F740F-5F4C-44FC-9CB2-DBD2350E3C1E
instance of	scholarly article
main subject	wds:Q73561096-EAABDD7E-7263-4468-B9A4-668E597C8505
main subject	glutathione
PubMed ID	wds:Q73561096-DA2EEADE-6F4E-4297-9C6A-82CB7E240116
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10722701
PubMed ID	10722701
published in	wds:Q73561096-26B58082-9C6C-4095-A1FA-211EEE4D30E4
published in	Journal of Biological Chemistry
issue	wds:Q73561096-7D2BD71A-2BA9-4CE9-9F7B-14A9A01C52CC
volume	wds:Q73561096-7D55C213-74A9-4F03-B663-E64B106DB2B4
issue	12
volume	275
DOI	wds:Q73561096-A5387D48-A1E9-4F18-A2F5-7C57B6CB792D
DOI	http://dx.doi.org/10.1074/JBC.275.12.8618
DOI	10.1074/JBC.275.12.8618
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73561096
is cites work of	Functional and structural roles of the glutathione-binding residues in maize (Zea mays) glutathione S-transferase I Human glutathione transferase T2-2 discloses some evolutionary strategies for optimization of the catalytic activity of glutathione transferases. An ensemble of theta class glutathione transferases with novel catalytic properties generated by stochastic recombination of fragments of two mammalian enzymes Enzymes of the cyclooxygenase pathways of prostanoid biosynthesis Structural Basis of the Catalytic Mechanism Operating in Open-Closed Conformers of Lipocalin Type Prostaglandin D Synthase Glutathione transferases are structural and functional outliers in the thioredoxin fold Identification and characterization of GSTT3, a third murine Theta class glutathione transferase A sensitive core region in the structure of glutathione S-transferases The conserved Asn49 of maize glutathione S-transferase I modulates substrate binding, catalysis and intersubunit communication Clarification of the role of key active site residues of glutathione transferase zeta/maleylacetoacetate isomerase by a new spectrophotometric technique A semisynthetic glutathione peroxidase with high catalytic efficiency. Selenoglutathione transferase.
is cites work of	wds:Q28345212-2E94500E-90A7-4B3E-942F-F1CCD14EE9F8 wds:Q27643949-EDD965AB-84B4-4985-BDBF-4F637E5E53D6 wds:Q31072499-B380410E-A374-4869-B91E-B11EE1D1F427 wds:Q43003136-BEE8D3D7-3271-47FB-A316-3CA1F7E39D97 wds:Q24655419-F42AB003-10CD-418D-9CE6-1848094D9D68

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