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Three-dimensional structures glutathione reductase

Glutathione reductase (GR) catalyzes the reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH) using NADPH provided from the hexose monophosphate pathway. GR, a ubiquitous flavoenzyme, maintains a high value of two for the GSH/GSSG ratio in the red blood cells. l,3-Bis(2-chloroethyl)-nitrosourea (BCNU) selectively inhibits cellular GR. GR is composed of two identical subunits, each of molecular mass 50 kDa (S8). The three-dimensional structure and mechanism of catalysis have been established for human GR (K17). [Pg.27]

Figure 15-10 The three-dimensional structure of glutathione reductase. Bound FAD is shown. NAD+ binds to a separate domain below the FAD. The two cysteine residues forming the reducible disulfide loop are indicated by dots. From Thieme et al.182... Figure 15-10 The three-dimensional structure of glutathione reductase. Bound FAD is shown. NAD+ binds to a separate domain below the FAD. The two cysteine residues forming the reducible disulfide loop are indicated by dots. From Thieme et al.182...
Thieme R, Pai EF, Schirmer RH, Schulz GE. Three-dimensional structure of glutathione reductase at 2 A resolution. J Mol Biol 1981 152 763-82. [Pg.642]

See other pages where Three-dimensional structures glutathione reductase is mentioned: [Pg.796]    [Pg.154]    [Pg.796]    [Pg.83]    [Pg.115]    [Pg.55]   
See also in sourсe #XX -- [ Pg.785 ]



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