Structural insight into acute intermittent porphyria

FASEB Journal

Volumn 23, Issue 2, 2009, Pages 396-404

  Song, Gaojie ^a   Li, Yang ^a   Cheng, Chongyun ^a   Zhao, Yu ^a   Gao, Ang ^a   Zhang, Rongguang ^b   Joachimiak, Andrzej ^b   Shaw, Neil ^a   Liu, Zhi Jie ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

Heme biosynthesis; Human porphobilinogen deaminase; Porphobilinogen hinge; X ray structure

Indexed keywords

DNA FRAGMENT; METHANE; PORPHOBILINOGEN DEAMINASE; PYRROLE;

ACUTE INTERMITTENT PORPHYRIA; ANIMAL CELL; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME STRUCTURE; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS;

BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROGEN BONDING; HYDROXYMETHYLBILANE SYNTHASE; MODELS, MOLECULAR; MUTATION; PORPHYRIA, ACUTE INTERMITTENT; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 59649123470     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.08-115469     Document Type: Article

References (39)

1. Furuyama, K., Kaneko, K., and Vargas, P. D. 5th (2007) Heme as a magnificent molecule with multiple missions: heme determines its own fate and governs cellular homeostasis. Tohoku J. Exp. Med. 213, 1-16
2. Granick, S., and Beale, S. I. (1978) Hemes, chlorophylls, and related compounds: biosynthesis and metabolic regulation. Adv. Enzymol. Relat. Areas Mol. Biol. 46, 33-203
3. Kauppinen, R. (2005) Porphyrias. Lancet 365, 241-252
4. Anderson, K., Sassa, S., Bishop, D., and Desnick, R. (2001) Disorders of heme biosynthesis: X-linked sideroblastic anemia and the porphyrias. In The Metabolic and Molecular Basis of Inherited Disease (Scriver, C. R., Beaudet, A. L., Sly, W. S., and Valle, D., eds) pp. 2991-3062, McGraw-Hill, New York, NY, USA
5. Woodard, S. I., and Dailey, H. A. (2000) Multiple regulatory steps in erythroid heme biosynthesis. Arch. Biochem. Biophys. 384, 375-378
6. Woodard, S. I., and Dailey, H. A. (1995) Regulation of heme biosynthesis in Escherichia coli. Arch. Biochem. Biophys. 316, 110-115
7. Meyer, U. A., and Schmid, R. (1978) The porphyrias. In The Metabolic Basis of Inherited Disease (Stanbury, J. B., Wyngaarden, J. B., and Fredrickson, D. S., eds) pp. 1166-1220, McGraw-Hill, New York, NY, USA
8. Kappas, A., Sassa, S., Galbraith, R. A., and Nordmann, Y. (1995) The porphyrias. In The Metabolic and Molecular Basis of Inherited Diseases (Scriver, C. R., Beaudet, A., Sly, W. S., and Valle, D., eds) pp. 2116-2127, McGraw-Hill, New York, NY, USA
9. Grandchamp, B. (1998) Acute intermittent porphyria. Semin Liver Dis. 18, 17-24
10. Puy, H., Deybach, J. C., Lamoril, J., Robreau, A. M., Silva, V. D., Gouya, L., Grandchamp, B., and Nordmann, Y. (1997) Molecular epidemiology and diagnosis of PBG deaminase gene defects in acute intermittent porphyria. Am. J. Hum. Genet. 60, 1373-1383
11. Strand, L. J., Meyer, U. A., Felsher, B. F., Redeker, A. G., and Marver, H. S. (1972) Decreased red cell uroporphyrinogen I synthetase activity in intermittent acute porphyria. J. Clin. Invest. 51, 2530-2536
12. Kauppinen, R., and Mustajoki, P. (1992) Prognosis of acute intermittent porphyria: occurrence of acute attacks, precipitating factors and associated disease. Medicine 71, 1-13
13. Grandchamp, B., Verneuil, H. D., Beaumont, C., Chretien, S., Walter, O., and Nordmann, Y. (1987) Tissue-specific expression of porphobilinogen deaminase: two isoenzymes from a single gene. Eur. J. Biochem. 162, 105-110
14. Jordan, P. M. (1996) Biosynthesis of tetrapyrroles. In New Comprehensive Biochemistry (Neuberger, A., and Van Deenen, L. L. M., eds) pp. 1-66, Elsevier, Amsterdam, The Netherlands
15. Warren, M. J., and Jordan, P. M. (1988) Investigation into the nature of substrate binding to the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase. Biochemistry 27, 9020-9030
16. Anderson, P. M., and Desnick, R. J. (1980) Purification and Properties of uroporphyrinogen I synthase from human erythrocytes. J. Biol. Chem. 225, 1993-1999
17. Louie, G. V., Brownlie, P. D., Lambert, R., Cooper, J. B., Blundell, T. L., Wood, S. P., Warren, M. J., Woodcock, S. C., and Jordan, P. M. (1992) Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site. Nature 359, 33-39
18. Stols, L., Gu, M., Dieckman, L., Raffen, R., Collart, F. R., and Donnelly, M. I. (2002) A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expr. Purif. 25, 8-15
19. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
20. Long, F., Vagin, A., Young, P., and Murshudov, G. (2008) BALBES: a molecular-replacement pipeline. Acta Crystallogr. D 64, 125-132
21. Adams, P. D., Grosse-Kunstleve, R. W., Hung, L. W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., and Terwilliger, T. C. (2002) PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954
22. Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132
23. Combet, C., Jambon, M., Deléage, G., and Geourjon, C. (2002) Geno3D: automatic comparative molecular modelling of protein. Bioinformatics 18, 213-214
24. Jones, R. M., and Jordan, P. M. (1994) Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana. Biochem. J. 299, 895-902
25. Correa-Garcia, S. R., Rossetti, M. V., and Batile, A. M. (1991) Studies on porphobilinogen-deaminase from Saccharomyces cerevisiae. Z. Naturforsch. C. 46, 1017-1023
26. Jordan, P. M., Thomas, S. D., and Warren, M. J. (1988) Purification, crystallization and properties of porphobilinogen deaminase from a recombinant strain of Escherichia coli K12. Biochem. J. 254, 427-435
27. Mazzetti, M. B., and Tomio, J. M. (1988) Characterization of porphobilinogen deaminase from rat liver. Biochim. Biophys. Acta 957, 97-104
28. Jordan, P. M., and Shemin, D. (1973) Purification and properties of uroporphyrinogen I synthetase from Rhodopseudomonas spheroides. J. Biol. Chem. 248, 1019-1024
29. Brons-Poulsen, J., Christiansen, L., Petersen, N., Horder, M., and Kristiansen, K. (2005) Characterization of two isoalleles and three mutations in both isoforms of purified recombinant human porphobilinogen deaminase. Scand. J. Clin. Lab. Invest. 65, 93-105
30. Jordan, P. M., Warren, M. J., and Awan, S. J. (1996) Discovery that the assembly of the dipyrromethane cofactor of porphobilinogen deaminase holoenzyme proceeds initially by the reaction of preuroporphyrinogen with the apoenzyme. Biochem. J. 316, 373-376
31. Woodcock, S. C., and Jordan, P. M. (1994) Evidence for participation ofaspartate-84 as a catalytic group at the active site of porphobilinogen deaminase obtained by site-directed mutagenesis of the hemC gene from Escherichia coli. Biochemistry 33, 2688-2695
32. Jordan, P. M., Al-Dbass, A., McNeill, L. A., Sarwar, M., and Butler, D. (2003) Human porphobilinogen deaminase mutations in the investigation of the mechanism of dipyrromethane cofactor assembly and tetrapyrrole formation. Biochem. Soc. T. 31, 731-735
33. Emekli, U., Schneidman-Duhovny, D., Wolfson, H. J., Nussinov, R., and Haliloglu, T. (2007) HingeProt: automated prediction of hinges in protein structures. Proteins 70, 1219-1227
34. Erlandsen, H., Fusetti, F., Martinez, A., Hough, E., Flatmark, T., and Stevens, R. C. (1997) Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nat. Struc. Mol. Biol. 4, 995-1000
35. Fusetti, F., Erlandsen, H., Flatmark, T., and Stevens, R. C. (1998) Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. J. Biol. Chem. 273, 16962-16967
36. Anderson, B. F., Baker, H. M., Norris, G. E., Rumball, S. V., and Baker, E. N. (1990) Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins. Nature 344, 784-787
37. Hrdinka, M., Puy, H., and Martasek, P. (2006) May 2006 update in porphobilinogen deaminase gene polymorphisms and mutations causing acute intermittent porphyria. Comparison with the situation in Slavic population. Physiol. Res. 55, 119-136
38. Matalon, R., Michals-Matalon, K., Koch, R., Grady, J., Tyring, S., and Stevens, R. C. (2005) Response of patients with phenylketonuria in the US to tetrahydrobiopterin. Mol. Genet. Metab. 86 (Suppl. 1), 17-21
39. Gamez, A., Wang, L., Sarkissian, C. N., Wendt, D., Fitzpatrick, P., Lemontt, J. F., Scriver, C. R., and Stevens, R. C. (2007) Structure-based epitope and PEGylation sites mapping of phenylalanine ammonia-lyase for enzyme substitution treatment of phenylketonuria. Molec. Genet. Metab. 91, 325-334