Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis

Biochemical Journal

Volumn 395, Issue 1, 2006, Pages 107-115

  Stines Chaumeil, Claire ^a   Talfournier, François ^a   Branlant, Guy ^a  

^a Biopôle de l Université de Lorraine   (France)

Author keywords

decarboxylation; Bicarbonate; CoA dependent aldehyde dehydrogenase (ALDH); Cysteine activation; Half of the sites reactivity; Lag phase

Indexed keywords

ACYLATION; CATALYSTS; PH EFFECTS;

APOENZYME; BICARBONATE; COA-DEPENDENT ALDEHYDE DEHYDROGENASE (ALDH); CYSTEINE ACTIVATION; DECARBOXYLATION; HALF-OF-THE-SITES REACTIVITY; LAG-PHASE; METHYLMALONATE SEMIALDEHYDE DEHYDROGENASE; TETRAMER;

ENZYMES;

APOENZYME; CYSTEINE; HOLOENZYME; MALONIC ACID DERIVATIVE; METHYLMALONATE SEMIALDEHYDE DEHYDROGENASE; METHYLMALONIC SEMIALDEHYDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; PROPIONYL COENZYME A; UNCLASSIFIED DRUG;

ACYLATION; AMINO ACID SEQUENCE; ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CORRELATION ANALYSIS; DECARBOXYLATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; NONHUMAN; OXIDATION; PH; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

2,2'-DIPYRIDYL; APOENZYMES; BACILLUS SUBTILIS; BICARBONATES; CATALYSIS; CYSTEINE; DECARBOXYLATION; DISULFIDES; HOLOENZYMES; HYDROGEN-ION CONCENTRATION; IODOACETAMIDE; KINETICS; METHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE (ACYLATING); MUTATION; NAD; OXIDATION-REDUCTION; PROTEIN BINDING; TIME FACTORS;

BACILLUS SUBTILIS;

EID: 33645644870     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051525     Document Type: Article

References (25)

1. Liu, Z. J., Sun, Y. J., Rose, J., Chung, Y. J., Hsiao, C. D., Chang, W. R., Kuo, I., Perozich, J., Lindahl, R., Hempel, J. and Wang, B. C. (1997) The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold. Nat. Struct. Biol. 4, 317-326
2. Steinmetz, C. G., Xie, P., Weiner, H. and Hurley, T. D. (1997) Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure 5, 701-711
3. Cobessi, D., Tete-Favier, F., Marchal, S., Azza, S., Branlant, G. and Aubry, A. (1999) Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. J. Mol. Biol. 290, 161-173
4. Farres, J., Wang, T. T., Cunningham, S. J. and Weiner, H. (1995) Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Biochemistry 34, 2592-2598
5. +-specific fatty aldehyde dehydrogenase from Vibrio harveyi. Biochemistry 34, 16725-16732
6. Wang, X. and Weiner, H. (1995) Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis. Biochemistry 34, 237-243
7. Vedadi, M. and Meighen, E. (1997) Critical glutamic acid residues affecting the mechanism and nuclotide specificity of Vibrio harveyi aldehyde dehydrogenase. Eur. J. Biochem. 246, 698-704
8. Marchal, S. and Branlant, G. (1999) Evidence for the chemical activation of essential cys-302 upon cofactor binding to nonphosphorylating glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans. Biochemistry 38, 12950-12958
9. Cobessi, D., Tete-Favier, F., Marchal, S., Branlant, G. and Aubry, A. (2000) Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. J. Mol. Biol. 300, 141-152
10. Marchal, S., Rahuel-Clermont, S. and Branlant, G. (2000) Role of glutamate-268 in the catalytic mechanism of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. Biochemistry 39, 3327-3335
11. Manjasetty, B. A., Powlowski, J. and Vrielink, A. (2003) Crystal structure of a bifunctionnal aldolase-dehydrogenase: sequestering a reactive and volatile intermediate. Proc. Natl. Acad. Sci. U.S.A. 100, 6992-6997
12. Steele, M. I., Lorenz, D., Hatter, K., Park, A. and Sokatch, J. R. (1992) Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase. J. Biol. Chem. 267, 13585-13592
13. Leal, N. A., Havemann, G. D. and Bobik, T. A. (2003) PduP is a coenzyme-A-acylating propionaldehyde dehydrogenase associated with the polyhedral bodies involved in B12-dependent 1,2-propanediol degradation by Salmonella entetica serovar Typhimurium LT2. Arch. Microbiol. 180, 353-361
14. Yoshida, K. I., Aoyama, D., Ishio, I., Shibayama, T. and Fujita, Y. (1997) Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis. J. Bacteriol. 179, 4591-4598
15. Kupiecki, F. P. and Coon, M. J. (1960) Methylmalonic semialdehyde. Biochem. Prep. 7, 69-71
16. Dubourg, H., Stines-Chaumeil, C., Didierjean, C., Talfournier, F., Rahuel-Clermont, S., Branlant, G. and Aubry, A. (2004) Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate- semialdehyde dehydrogenase from Bacillus subtilis. Acta Crystallogr. D. Biol. Crystallogr. D60, 1435-1437
17. Mellor, G. W., Thomas, E. W., Topham, C. M. and Brocklehurst, K. (1993) Ionization characteristics of the Cys-25/His-159 interactive system and of the modulatory group of papain: resolution of ambiguity by electronic perturbation of the quasi-2-mercaptopyridine leaving group in a new pyrimidyl disulphide reactivity probe. Biochem. J. 290, 289-296
18. Liu, M., Sergienko, E. A., Guo, F., Wang, J., Tittmann, K., Hübner, G., Furey, W. and Jordan, F. (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions. Biochemistry 40, 7355-7368
19. Hurley, T. D., Perez-Miller, S. and Breen, H. (2001) Order and disorder in mitochondrial aldehyde dehydrogenase. Chem. Biol. Interact. 130-132, 3-14
20. Dickinson, F. M. (2003) Conformational changes and activation of yeast aldehyde dehydrogenase by various agents. Chem. Biol. Interact. 143-144, 169-174
21. 2+-activated cytosolic aldehyde dehydrogenase of Saccharomyces cerevisiae. Biochem. J. 315, 393-399
22. Zhou, J. and Weiner, H. (2000) Basis of half-of-the-sites reactivity and the dominance of the K487 oriental subunit over the E487 subunit in heterotetrameric human liver mitochondrial aldehyde dehydrogenase. Biochemistry 39, 12019-12024
23. Shone, C. C. and Fromm, H. J. (1981) Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli. Biochemistry 20, 7494-7501
24. Söhling, B. and Gottschalk, G. (1993) Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri. Eur. J. Biochem. 212, 121-127
25. Witkowski, A., Joshi, A. K. and Smith, S. (2002) Mechanism of the β-ketoacyl synthase reaction catalyzed by the animal fatty acid synthase. Biochemistry 41, 10877-10887