The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity

FEBS Letters

Volumn 582, Issue 20, 2008, Pages 3090-3096

  Tang, Wai Kwan ^a   Wong, Kam Bo ^a   Lam, Yuk Man ^a   Cha, Sun Shin ^b   Cheng, Christopher H K ^a   Fong, Wing Ping ^a  

^a CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

^b Korea Research Institute of Ships and Ocean Engineering   (South Korea)

Author keywords

Aminoadipic semialdehyde; ALDH7; Antiquitin; Pyridoxine dependent epilepsy; Site directed mutagenesis; X ray crystallography

Indexed keywords

ALDEHYDE DEHYDROGENASE; ALDEHYDE DERIVATIVE; ALPHA AMINOADIPIC SEMIALDEHYDE; ANTIQUITIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; PYRIDOXINE;

ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SPECIFICITY; EPILEPSY; FISH; GENE MUTATION; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; SEABREAM; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

2-AMINOADIPIC ACID; ALDEHYDE DEHYDROGENASE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; EPILEPSY; FISH PROTEINS; HUMANS; MUTATION; NAD; PROTEIN CONFORMATION; PYRIDOXINE; SEA BREAM; SUBSTRATE SPECIFICITY;

EID: 49649114051     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.07.059     Document Type: Article

References (39)

1. Sophos N.A., Black W.J., and Vasiliou V. An update of the ALDH gene family. In: Weiner H., Plapp B., Lindahl R., and Maser E. (Eds). Enzymology and Molecular Biology of Carbonyl Metabolism Vol. 12 (2006), Purdue University Press, Indiana 3-7
2. Lee P., Kuhl W., Gelbart T., Kamimura T., West C., and Beutler E. Homology between a human protein and a protein of the green garden pea. Genomics 21 (1994) 371-378
3. Fong W.P., Cheng C.H.K., and Tang W.K. Antiquitin, a relatively unexplored member in the superfamily of aldehyde dehydrogenases with diversified physiological functions. Cell. Mol. Life Sci. 63 (2006) 2881-2885
4. Guerrero F.D., Jones J.T., and Mullet J.E. Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes. Plant Mol. Biol. 15 (1990) 11-26
5. Stroeher V.L., Boothe J.G., and Good A.G. Molecular cloning and expression of a turgor-responsive gene in Brassica napus. Plant Mol. Biol. 27 (1995) 541-551
6. Kirch H.H., Schlingensiepen S., Kotchoni S., Sunkar R., and Bartels D. Detailed expression analysis of selected genes of the aldehyde dehydrogenase (ALDH) gene superfamily in Arabidopsis thaliana. Plant Mol. Biol. 57 (2005) 315-332
7. Rodrigues S.M., Andrade M.O., Gomes A.P., Damatta F.M., Baracat-Pereira M.C., and Fontes E.P. Arabidopsis and tobacco plants ectopically expressing the soybean antiquitin-like ALDH7 gene display enhanced tolerance to drought, salinity, and oxidative stress. J. Exp. Bot. 57 (2006) 1909-1918
8. Tang W.K., Chan C.B., Cheng C.H.K., and Fong W.P. Seabream antiquitin: molecular cloning, tissue distribution, subcellular localization and functional expression. FEBS Lett. 579 (2005) 3759-3764
9. Wong W.Y., Cheng C.H.K., and Fong W.P. Lack of inducibility of antiquitin (ALDH7A1) in cultured human embryonic kidney (HEK293) cell under osmotic or oxidative stress. In: Weiner H., Plapp B., Lindahl R., and Maser E. (Eds). Enzymology and Molecular Biology of Carbonyl Metabolism Vol. 12 (2006), Purdue University Press, Indiana 96-103
10. Ellederova Z., Halada P., Man P., Kubelka M., Motlik J., and Kovarova H. Protein patterns of pig oocytes during in vitro maturation. Biol. Reprod. 71 (2004) 1533-1539
11. Yamada K., Mori H., and Yamaki S. Identification and cDNA cloning of a protein abundantly expressed during apple fruit development. Plant Cell Physiol. 40 (1999) 198-204
12. Tang W.K., Cheng C.H.K., and Fong W.P. First purification of the antiquitin protein and demonstration of its enzymatic activity. FEBS Lett. 516 (2002) 183-186
13. Chan W.M., Tang W.K., Cheng C.H.K., and Fong W.P. Purification, N-terminal sequence determination and enzymatic characterization of antiquitin from the liver of grass carp. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 136 (2003) 443-450
14. Mills P.B., et al. Mutations in antiquitin in individuals with pyridoxine-dependent seizures. Nat. Med. 12 (2006) 307-309
15. Plecko B., et al. Biochemical and molecular characterization of 18 patients with pyridoxine-dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene. Hum. Mutat. 28 (2007) 19-26
16. Perozich J., Nicholas H., Wang B.C., Lindahl R., and Hempel J. Relationships within the aldehyde dehydrogenase extended family. Protein Sci. 8 (1999) 137-146
17. Liu Z.J., et al. The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold. Nat. Struct. Biol. 4 (1997) 317-326
18. Moore S.A., Baker H.M., Blythe T.J., Kitson K.E., Kitson T.M., and Baker E.N. Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases. Structure 6 (1998) 1541-1551
19. Lamb A.L., and Newcomer M.E. The structure of retinal dehydrogenase type II at 2.7 Å resolution: implications for retinal specificity. Biochemistry 38 (1999) 6003-6011
20. Steinmetz C.G., Xie P., Weiner H., and Hurley T.D. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure 5 (1997) 701-711
21. Johansson K., El-Ahmad M., Ramaswamy S., Hjelmqvist L., Jornvall H., and Eklund H. Structure of betaine aldehyde dehydrogenase at 2.1 Å resolution. Protein Sci. 7 (1998) 2106-2117
22. Gruez A., Roig-Zamboni V., Grisel S., Salomoni A., Valencia C., Campanacci V., Tegoni M., and Cambillau C. Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase. J. Mol. Biol. 343 (2004) 29-41
23. Inagaki E., Ohshima N., Takahashi H., Kuroishi C., Yokoyama S., and Tahirov T. Crystal structure of Thermus thermophilus delta(1)-pyrroline-5-carboxylate dehydrogenase. J. Mol. Biol. 362 (2006) 490-501
24. D'Ambrosio K., Pailot A., Talfournier F., Didierjean C., Benedetti E., Aubry A., Branlant G., and Corbier C. The first crystal structure of a thioacylenzyme intermediate in the ALDH family: new coenzyme conformation and relevance to catalysis. Biochemistry 45 (2006) 2978-2986
25. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276 (1997) 307-326
26. Vagin A.A., and Isupov M.N. Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1451-1456
27. Collaborative Computational Project, N. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
28. Cheung Y.Y., Allen M.D., Bycroft M., and Wong K.B. Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1308-1310
29. McRee D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
30. Brunger A.T., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
31. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53 (1997) 240-255
32. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2126-2132
33. Kleywegt G.J., and Brünger A.T. Checking your imagination: applications of the free R value. Structure 4 (1996) 897-904
34. Fabiola F., Korostelev A., and Chapman M.S. Bias in cross-validated free R factors: mitigation of the effects of non-crystallographic symmetry. Acta Crystallogr. D Biol. Crystallogr. 62 (2006) 227-238
35. Soda K., Misono H., and Yamamoto T. l-Lysine:alpha-ketoglutarate aminotransferase. I. Identification of a product, delta-1-piperideine-6-carboxylic acid. Biochemistry 7 (1968) 4102-4109
36. Bateman O.A., Purkiss A.G., van Montfort R., Slingsby C., Graham C., and Wistow G. Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens. Biochemistry 42 (2003) 4349-4356
37. Perez-Miller S.J., and Hurley T.D. Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase. Biochemistry 42 (2003) 7100-7109
38. Ni L., Sheikh S., and Weiner H. Involvement of glutamate 399 and lysine 192 in the mechanism of human liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 272 (1997) 18823-18826
39. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291