Amino acid substitutions at the dimer interface of human glucose-6-phosphate dehydrogenase that increase thermostability and reduce the stabilising effect of NADP

European Journal of Biochemistry

Volumn 251, Issue 1-2, 1998, Pages 382-388

  Scopes, Deborah A ^a   Bautista, José M ^b   Naylor, Claire E ^c   Adams, Margaret J ^c   Mason, Philip J ^a  

^a HAMMERSMITH HOSPITAL   (United Kingdom)

^b UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Dimer interface; Glucose 6 phosphate dehydrogenase; Thermostability

Indexed keywords

DIMER; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME STABILITY; ENZYME STRUCTURE; LEUCONOSTOC; NONHUMAN; PRIORITY JOURNAL; THERMOSTABILITY;

EID: 0032518592     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2510382.x     Document Type: Article

References (27)

1. Beutler, E. (1994) G6PD deficiency, Blood 84, 3613-3636.
2. Naylor, C. E., Rowland, P., Basak, A. K., Gover, S., Mason, P. J., Bautista, J. M., Vulliamy, T. J., Luzzatto, L. & Adams, M. J. (1996) Glucose-6-phosphate-dehydrogenase mutations causing enzyme deficiency in a model of the tertiary structure of the human enzyme, Blood 87, 2974-2982.
3. Rowland, P., Basak, A. K., Gover, S., Levy, H. R. & Adams, M. J. (1994) The three dimensional structure of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2 A resolution, Structure 2, 1073-1087.
4. Cohen, P. & Rosemeyer, M. A. (1969) Subunit interactions of human glucose-6-phosphate dehydrogenase from human erythrocytes, Eur. J. Biochem. 8, 8-15.
5. Yoshida, A. & Hoagland, V. D. J. (1970) Active molecular unit and NADP content of human glucose 6-phosphate dehydrogenase, Biochem. Biophys. Res. Commun. 40, 1167-1172.
6. Bonsignore, A., Lorenzoni, I., Cancedda, R., Consulich, M. E. & De Flora, A. (1971) Effect of divalent cations on the structure of human erythrocyte G6PD, Biochem. Biophys. Res. Commun. 42, 159-170
7. Cancedda, F., Ogunmola, G. B. & Luzzatto, L. (1973) Genetic variants of human erythrocyte glucose-6-phosphate-dehydrogenase. Discrete conformational states stabilized by NADP+ and NADPH, Eur. J. Biochem. 34, 199-204.
8. Beutler, E., Vulliamy, T. & Luzzatto, L. (1996) Hematologically important mutations - glucose-6-phosphate dehydrogenase, Blood Cells Mol. Dis. 22, 49-56.
9. Ruwende, C., Khoo, S. C., Snow, R. W., Yates, S., Kwiatkowski, D., Gupta, S., Warn, P., Allsopp, C., Gilbert, S. C., Peschu, N., Newbold, C. I., Greenwood, B. M., Marsh, K. & Hill, A. (1995) Natural selection of hemi- and heterozygotes for G6PD deficiency in Africa by resistance to severe malaria, Nature 376, 246-249.
10. Thomas, P. J., Qu, B.-H. & Pedersen, P. L. (1995) Defective protein folding as a basis of human disease, Trends Biochem. Sci. 20, 456-459.
11. Gómez-Gallego, F., Garrido-Pertierra, A., Mason, P. J. & Bautista, J. M. (1996) Unproductive folding of the human G6PD deficient variant A-. FASEB J. 10, 153-158.
12. Goward, C. R., Miller, J., Nicholls, D. J., Irons, L. I., Scawen, M. D., O'Brien, R. & Chowdhry, B. Z. A. (1994) Single amino-acid mutation enhances the thermal stability of Escherichia coli malate-dehydrogenase, Eur. J. Biochem. 224, 249-255.
13. Beutler, E., Kuhl, W., Gelbart, T. & Forman, L. (1991) DNA-sequence abnormalities of human glucose-6-phosphate-dehydrogenase variants, J. Biol. Chem. 266, 4145-4150.
14. Hirono, A., Fujii, H., Hirono, K., Kanno, H. & Miwa, S. (1992) Molecular abnormality of a Japanese glucose-6-phosphate-dehydrogenase variant (G6PD Tokyo) associated with hereditary non-spherocytic hemolytic-anemia, Hum. Genet. 88, 347-348.
15. Kirkman, H. & Hendrikson, E. (1962) G6PD from human erythrocytes II: subactive states of the enzyme from normal persons, J. Biol. Chem. 237, 2371-2376.
16. Luzzatto, L. & Allan, N. C. (1965) Different properties of glucose-6-phosphate dehydrogenase from human erythrocytes with normal and abnormal enzyme levels, Biochem. Biophys. Res. Commun. 21, 547-554.
17. Bautista, J. M., Fuentes, J. M., Diez, A., Gutierrezmerino, C. &. Soler, G. (1992) Unfolding and trypsin inactivation studies reveal a conformation drift of glucose-6-phosphate-dehydrogenase upon binding of NADP, Biochim. Biophys. Acta 1122, 99-106.
18. Bautista, J. M., Garrido-Pertierra, A. & Soler, G. (1988) Glucose-6-phosphate-dehydrogenase from dicentrarchus-labrax liver - kinetic mechanism and kinetics of NADPH inhibition, Biochim. Biophys. Acta 967, 354-363.
19. Sambrook, J., Fritsch, E. & Maniatis, T. (1989) Molecular cloning: a laboratory manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
20. Town, M., Bautista, J. M., Mason, P. J. & Luzzatto, L. (1992) Both mutations in G6PD A- are necessary to produce the G6PD deficient phenotype, Hum. Mol. Genet. 1, 171-174.
21. Bautista, J. M., Mason, P. J. & Luzzatto, L. (1992) Purification and properties of human glucose-6-phosphate-dehydrogenase made in Escherichia coli, Biochim. Biophys. Acta 1119, 74-80.
22. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
23. Fraenkel, D. (1968) Selection of Escherichia coli mutants lacking glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase. J. Bacteriol. 95, 1267-1271.
24. Gomez-Gallego, F., Garrido-Pertierra, A. & Bautista, J. M. (1995) Protein disulphide isomerase assisted folding of human glucose-6-phosphate dehydrogenase, Biochem. Soc. Trans. 23, 82S.
25. Beutler, E. (1986) G-6-PD Walter Reed: possible insight into "structural" NADP in G-6-PD, Am. J. Hematol. 23, 25-30.
26. Hirono, A., Kuhl, W., Gelbart, T., Forman, L., Fairbanks, V. F. & Beutler, E. (1989) Identification of the binding domain for NADP of human glucose-6-phosphate dehydrogenase by sequence analysis of mutants, Proc. Natl Acad. Sci. USA 86, 10 015-10 017.
27. Kolik, M. & Zuber, H. (1993) Mutations that significantly change the stability, flexibility and quaternary structure of the L-lactate dehydrogenase from Bacillus megaterium, Eur. J. Biochem. 211, 267-280.