Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase.
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The interaction of the chemotherapeutic drug chlorambucil with human glutathione transferase A1-1: kinetic and structural analysisA Glutathione Transferase from Agrobacterium tumefaciens Reveals a Novel Class of Bacterial GST SuperfamilyThe three-dimensional structure of a class-Pi glutathione S-transferase complexed with glutathione: the active-site hydration provides insights into the reaction mechanismFunctional and structural roles of the glutathione-binding residues in maize (Zea mays) glutathione S-transferase IRat glutathione S-transferase M4-4: an isoenzyme with unique structural features including a redox-reactive cysteine-115 residue that forms mixed disulphides with glutathioneStructure-activity relationships for chemical and glutathione S-transferase-catalysed glutathione conjugation reactions of a series of 2-substituted 1-chloro-4-nitrobenzenesMeasurement of intrinsic rate constants in the tyrosine hydroxylase reactionGlobal Kinetic Mechanism of Microsomal Glutathione Transferase 1, insights into dynamic enzyme activation.Forced evolution of glutathione S-transferase to create a more efficient drug detoxication enzyme.Homology modeling of cephalopod lens S-crystallin: a natural mutant of sigma-class glutathione transferase with diminished endogenous activityMacromolecular Crystallography and Structural Biology Databases at NIST.Comparison of epsilon- and delta-class glutathione S-transferases: the crystal structures of the glutathione S-transferases DmGSTE6 and DmGSTE7 from Drosophila melanogaster.Mutagenic analysis of conserved arginine residues in and around the novel sulfate binding pocket of the human Theta class glutathione transferase T2-2.Characterization of the binding of 8-anilinonaphthalene sulfonate to rat class Mu GST M1-1.Crystal structure of a theta-class glutathione transferase.Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their site-directed mutants heterologously expressed in Escherichia coli: identification of Lys-15 and Ser-208 on cGSTA1-1 as residues interacting with etCatalysis of Silver catfish Major Hepatic Glutathione Transferase proceeds via rapid equilibrium sequential random Mechanism.Steady-state kinetics and chemical mechanism of octopus hepatopancreatic glutathione transferase.Modification of glutathione S-transferase 3-3 mutants with 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone. Identification of the C-terminal tryptic fragment as part of the H-site and evidence that 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquiMutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues.Amino acid sequence of glutathione S-transferase rGSTM5* from rat testis.Glutamate-64, a newly identified residue of the functionally conserved electron-sharing network contributes to catalysis and structural integrity of glutathione transferasesCatalytic and structural contributions for glutathione-binding residues in a Delta class glutathione S-transferase.A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis.Cys-X scanning for expansion of active-site residues and modulation of catalytic functions in a glutathione transferase.Contribution of the mu loop to the structure and function of rat glutathione transferase M1-1.Delineation of xenobiotic substrate sites in rat glutathione S-transferase M1-1.Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production.
P2860
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P2860
Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Tyrosine 115 participates both ...... f a glutathione S-transferase.
@en
Tyrosine 115 participates both ...... f a glutathione S-transferase.
@nl
type
label
Tyrosine 115 participates both ...... f a glutathione S-transferase.
@en
Tyrosine 115 participates both ...... f a glutathione S-transferase.
@nl
prefLabel
Tyrosine 115 participates both ...... f a glutathione S-transferase.
@en
Tyrosine 115 participates both ...... f a glutathione S-transferase.
@nl
P2093
P1476
Tyrosine 115 participates both ...... of a glutathione S-transferase
@en
P2093
P304
11508-11511
P407
P577
1993-06-01T00:00:00Z