Abstract
Glutathione plays a critical role in the maintenance of reduced thiol groups in the cell and is of particular importance in the biosynthesis of DNA [for a review, see Holmgren, 1985]. Glutathione itself is maintained in a reduced form at the expense of NADPH by the action of the enzyme glutathione reductase (EC 1.6.4.2):
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Berry, A., Scrutton, N.S. and Perham, R.N., 1989, Switching kinetic mechanism and putative proton donor by directed mutagenesis of glutathione reductase, Biochemistry 28:1264.
Brown, N. L., Ford, S. J., Pridmore, D. and Fritzinger, D. C., 1983, Nucleotide sequence of a gene from the Pseudomonas transposon Tn501 encoding mercuric reductase, Biochemistry 22:4089.
Creighton, T.E., 1988, Disulphide bonds and protein stability, BioEssays 8:57.
Deonarain, M.P., Berry, A., Scrutton, N.S. and Perham, R.N., 1989, Alternative proton donors/acceptors in the catalytic mechanism of the glutathione reductase of Escherichia coli: the role of His-439 and Tyr-99, Biochemistry x in press.
Fox, B. and Walsh, C.T., 1982, Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reductionOactive disulphide, J. Biol Chem. 257:2498.
Fox, B. and Walsh, C.T., 1983, Mercuric reductase: Homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide, Biochemistry 22:4082.
Greer, S. and Perham, R.N., 1986, Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulphide oxidoreductases, Biochemistry 25:2736.
Holmgren, A., 1985, Thioredoxin, Annu. Rev. Biochem. 54:237.
Jaenicke, R., 1987, Folding and association of proteins, Progress in Biophys. and Mol. Biol. 49:117.
Karplus, P.A. and Schulz, G.E., 1987, Refined structure of glutathione reductase as 1.54 Å resolution, J. Mol. Biol. 195:701.
Karplus, P.A., Pai, E.F. and Schulz, G.E., 1989, A crystallographic study of the glytathione binding site of glytathione reductase at 0.3nm resolution, Eur. J. Biochem. 178:693.
Krauth-Siegel, R.L., Blatterspiel, R., Saleh, M., Schulz, G.E., Schirmer, R.H. and Untucht-Grau, R., 1982, Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain, Eur. J. Biochem. 121:259.
Krauth-Siegel, R.L., Enders, B., Henderson, G.B., Fairlamb, A.H. and Schirmer, H.R., 1987, Trypanothione reductase from Trypanosoma cruzi. Purification and characterization of the crystalline enzyme, Eur. J. Biochem. 164:123.
Mannervik, B., 1973, A branching mechanism of glutathione reductase, Biochem. Biophys. Res. Commun. 53:1151.
Matthews, R. G., Ballou, D. P., Thorpe, C. and Williams, C. H., Jr., 1977, Ion pair formation in pig heart lipoamide dehydrogenase. Rationalization of pH profiles for reactivity of oxidized enzyme with dihydrolipoamide and 2-electron-reduced enzyme with lipoamide and iodoacetamide, J. Biol. Chem. 252:3199.
Packman, L.C. and Perham, R.N., 1982, An amino acid sequence in the active site of lipoamide dehydrogenase from Bacillus stearothermophilus, FEBS Lett. 139:155.
Pai, E.F. and Schulz, G.E., 1983, The catalytic mechanism of glytathione reductase as derived from X-ray diffraction analyses of reaction intermediates, J. Mol. Biol. 258:1751.
Perham, R.N., Harrison, R.A. and Brown, J.P., 1978, The lipoamide dehydrogenase component of the 2-oxo acid dehydrogenase multienzyme complexes of Escherichia coli, Biochem. Soc. Trans. 6:47.
Perham, R.N., Packman, L.C. and Radford, S.E., 1987, 2-Oxo acid dehydrogenase multienzyme complexes: in the beginning and halfway there, in: “Kreb’s citric acid cycle -half a centry and still turning,” J. Kay and P.D.J. Weitzman, eds., Biochem. Soc. Symp. 54:67.
Perry, L.J., and Wetzel, R., 1986, Unpaired cysteine-54 interferes with the ability of an engineered disulfide to stabilize T4 lysozyme, Biochemistry 25:733.
Reed, L.J., 1974, Multienzyme complexes, Ace. Chem. Res. 7:40.
Rice, D.W., Schulz, G.E. and Guest, J.R., 1984, Structural relationship between glutathione reductase and lipoamide dehydrogenase, J. Mol. Biol. 174:483.
Rüssel, M. and Model, P., 1988, Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulphide oxidoreductases, J. Biol. Chem. 263:9015.
Sauer, R.T., Hehir, K., Stearman, R.S., Weiz, M.A., Jeitler-Nilsson, A., Suchanek, E.G., and Pabo, C.O., 1986, An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of λ-repressor, Biochemistry 25:5992.
Schierbeek, A.J., Swarte, M.B.A., Dijksta, B.W., Vriend, G., Read, R.J., Hol, W.G.J., Drenth, J. and Betzel, C., 1989, X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques, J. Mol. Biol. 206:365.
Scrutton, N.S., Berry, A. and Perham, R.N., 1987, Purfication and characterization of glutathione reductase encoded by a cloned and over-expressed gene in Escherichia coli, Biochem. J. 245:875.
Scrutton, N.S., Berry, A. and Perham, R.N., 1988, Engineering of an intersubunit disulphide bridge in glutathione reductase from Escherichia coli, FEBS Lett. 24:46.
Shames, S.L., Fairlamb, A.H., Cerami, A. and Walsh, C.T., 1986, Purification and characterization of trypanothione reductase from Crithidiafasciculata, a newly discovered member of the family of disulphide-containing flavoprotein reductases, Biochemistry 25:3519.
Shames, S.L., Kimmel, B.E., Peoples, O.P., Agabian, N. and Walsh, C.T., 1988, Trypanothione reductase of Trypanosoma congolense: Gene isolation, primary sequence determination, and comparison to glutathione reductase, Biochemistry 27:5014.
Shaw, W.V., 1987, Protein Engineering. The design, synthesis and characterization of fictitious proteins, Biochem. J. 246:1.
Stephens, P.E., Lewis, H.M., Darlison, M.G. and Guest, J.R., 1983, Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12, Eur. J. Biochem. 135:519.
Thieme, R., Pai, E.F., Schirmer, R.H. and Schulz, G.E., 1981, Three-dimensional structure of glutathione reductase at 2 Å resolution J. Mol. Biol. 151:763.
Wells, J.A. and Powers, D.B., 1986, In vivo formation and stability of engineered disulfide bonds in subtilisin, J. Biol. Chem. 261:6564.
Wetzel, R., Perry, L.J., Baase, W.A. and Becktel, W.J., 1988, Disulfide bonds and thermal stability in T4 lysozyme, Proc. Natl. Acad. Sci. U.S.A. 85:401.
Williams, C.H., Jr., 1976, Flavin containing dehydrogenases, in: “The Enzymes” 3rd edn., P.D. Boyer, ed., Academic Press, New York. 13:89.
Williams, C.H., Jr., Arscott, L.D. and Schulz, G.E., 1982, Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase, Proc. Natl. Acad. Sci. U.S.A. 79:2199.
Wong, K.K., Vanoni, M.A. and Blanchard, J.S., 1988, Glutathione reductase: Solvent equilibrium and kinetic isotope effects, Biochemistry 27:7091.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1989 Plenum Press, New York
About this chapter
Cite this chapter
Perham, R.N., Berry, A., Scrutton, N.S., Deonarain, M.P. (1989). Site-Directed Mutagenesis and the Mechanism of Flavoprotein Disulphide Oxidoreductases. In: Jardetzky, O., Holbrook, R. (eds) Protein Structure and Engineering. NATO ASI Series, vol 183. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5745-2_21
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5745-2_21
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5747-6
Online ISBN: 978-1-4684-5745-2
eBook Packages: Springer Book Archive