A gene cluster encoding malonyl-CoA decarboxylase (MatA), malonyl-CoA synthetase (MatB) and a putative dicarboxylate carrier protein (MatC) in Rhizobium trifolii - Cloning, sequencing, and expression of the enzymes in Escherichia coli

European Journal of Biochemistry

Volumn 257, Issue 2, 1998, Pages 395-402

  An, Jae Hyung ^a   Kim, Yu Sam ^a  

^a Yonsei University   (South Korea)

Author keywords

Malonyl CoA decarboxylase; Malonyl CoA synthetase; MatABC; Putative dicarboxylate carrier proteins; Rhizobium trifolii

Indexed keywords

ACETYL COENZYME A; BACTERIAL ENZYME; BACTERIAL PROTEIN; CARRIER PROTEIN; DICARBOXYLIC ACID; DNA; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MALONIC ACID; MALONYL COENZYME A; MALONYL COENZYME A DECARBOXYLASE; MALONYL COENZYME A SYNTHETASE; MEMBRANE PROTEIN; POLYPEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; DNA SEQUENCE; ESCHERICHIA COLI; GENE CLUSTER; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN EXPRESSION; RHIZOBIUM TRIFOLII; THIN LAYER CHROMATOGRAPHY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; HAEMOPHILUS INFLUENZAE; PROKARYOTA; RHIZOBIUM LEGUMINOSARUM; RHIZOBIUM TRIFOLII; TRIFOLIUM;

EID: 0032532250     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2570395.x     Document Type: Article

References (36)

1. Bentley, L. E. (1952) Occurrence of malonic acid in plants, Nature 170, 847-848.
2. Stumpf, D. K. & Burris, R. H. (1981) Organic acid content of soybean: age and source of nitrogen, Plant Physiol. 68, 989-991.
3. Streeter, J. G. (1987) Carbohydrate, organic acid, and amino acid composition of bacteroids and cytosol from soybean nodules, Plant Physiol. (Bethesda) 85, 768-773.
4. Kim, Y. S. & Chae, H. Z. (1991) Purification and properties of malonyl-CoA synthetase from Rhizobium japonicum, Biochem. J. 273, 511-516.
5. Kim, Y. S. & Kang, S. W. (1994) Steady-state kinetics of malonyl-CoA synthetase from Bradyrhizobium japonicum and evidence for malonyl-AMP formation in the reaction. Biochem. J. 297, 327-333.
6. Kim, Y. S., Kwon, S. J. & Kang, S. W. (1993) Malonyl-CoA synthetase from Rhizobium trifolii, Biochem. J. 26, 176-183.
7. Kang, S. W., Hong, S. Y., Ryoo, H. D., Rhyu, K. I. & Kim, Y. S. (1994) Kinetics of malonyl-CoA synthetase from Rhizobium trifolii and evidences for malonyl-AMP formation as a reaction intermediate, Bull. Korean Chem. Soc. 15, 394-399.
8. Kim, Y. S. & Chae, H. Z. (1990) A model of nitrogen flow by malonamate in Rhizobium japonicum, Biochem. Biophy. Res. Commun. 169, 692-699.
9. Kang, S. W. & Kim, Y. S. (1996) Evidence that Bradyrhizobium japonicum bacteroid and plant cytosolic malonamidase E2 (MAE2) in soybean nodules are identical. J. Plant Physiol. 149, 290-294.
10. Kim, Y. S., Chae, H. Z., Lee, E. & Kim, Y. S. (1991) Identification of malonate specific enzymes, malonyl-CoA synthetase and malonamidase, in Rhizobia, Korean J. Microbiol. 29, 40-48.
11. Kim, Y. S. & Kolattukudy, P. E. (1978) Malonyl-CoA decarboxylase from the uropygial gland of waterfowl: purification, properties, immunological comparison, and role in regulating the synthesis of multimethyl-branched fatty acids, Arch. Biochem. Biophys. 190, 585-597.
12. Kim, Y. S. & Kolattukudy, P. E. (1978) Purification and properties of malonyl-CoA decarboxylase from rat liver mitochondria and its immunological comparison with the enzymes from rat brain, heart, and mammary gland, Arch. Biochem. Biophys. 190, 224-246.
13. 12 by methylmalonyl Coenzyme A mutase, J. Biol. Chem. 248, 1445-1450.
14. Scrutton, M. C. & Utter, M. F. (1967) Pyruvate carboxylase IX, some properties of the activation by certain acyl derivatives of coenzyme A, J. Biol. Chem. 242, 1723-1735.
15. Hunaiti, A. R. & Kolattukudy, P. E. (1984) Malonyl-CoA decarboxylase from Streptomyces erythreus: purification, properties, and possible role in the production of erythromycin, Arch. Biochem. Biophys. 229, 426-439.
16. Hsieh, Y. J. & Kolattukudy, P. E. (1994) Inhibition of erythromycin synthesis by disruption of malonyl-coenzyme A decarboxylase gene eryM in Saccharopolyspora erythraea, J. Bacteriol. 176, 714-724-20.
17. Bott, M., Pfister, K., Burda, P., Kalbermatter, O., Woehlke, G. & Dimroth, P. (1997) Methylmalonyl-CoA decarboxylase from Propionigenium modestum: cloning and sequencing of the structural genes and purification of the enzyme complex, Eur. J. Biochem. 250, 590-599.
18. Samhrook, J., Fritsch, E. F. & Maniatis, T. (1989) Molecular cloning: a laboratory manual, 2nd edn, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
19. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
20. Kim, Y. S. & Bang, S. K. (1988) Assays for malonyl-Coenzyme A synthase, Anal. Biochem. 170, 45-49.
21. Kolattukudy, P. E., Poulose, A. J. & Kim, Y. S. (1981) Malonyl-CoA decarboxylase from avian, mammalian, and microbial sources, Methods Enzymol. 71C, 150-153.
22. Giddings, J. C. (1993) Field-flow fractionation: analysis of macromolecular, colloidal, and particulate materials, Science 260, 1456-1465.
23. Anke, H. & Spector, L. B. (1975) Evidence for an acetyl-enzyme intermediate in the action of acetyl-CoA synthetase, Biochem. Biophys. Res. Commun. 67, 767-773.
24. Fuldam, M., Heinz, E. & Wolter, F. P. (1994) The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family, Mol. Gen. Genet. 242, 241-249.
25. Fleischmann, R. D., Adams, M. D., White, O., Clayton, R. A., Kirkness, E. F., Kerlavage, A. R., Bult, C. L. Tomb, J. F., Dougherty, B. A., Merrick, J. M., McKenney, K., Sutton, G., FitzHugh, W., Fields, C. A., Gocayne, J. D., Scott, J. D., Shirley, R., Liu, L. I., Glodek, A., Kelley, J. M., Weidman, J. F., Phillips, C. A., Spriggs, T., Hedblom, E., Cotton, M. D., Utterback, T. R., Hanna, M. C., Nguyen, D. T., Saudek, D. M., Brandon, R. C., Fine, L. D., Fritchman, J. L., Fuhrmann, J. L., Geoghagen, N. S. M., Gnehm, C. L., McDonald, L. A., Small, K. V., Fraser, C. M. Smith, H. O. & Venter, J. C. (1995) Whole-genome random sequencing and assembly of Haemophilus influenzae Rd, Science 269, 496-512.
26. Blobel, F. & Erdmann, R. (1996) Identification of a yeast peroxisomal member of the family of AMP-binding protein, Eur. J. Biochem. 240, 468-476.
27. Jang, S. H., Cheesbrough, T. M. & Kolattukudy, P. E. (1989) Molecular cloning, nucleotide sequence and tissue distribution of malonyl-CoA decarboxylase, J. Biol. Chem. 264, 3500-3505.
28. 4-dicarboxylase membrane transporters (DcuA and DcuB) distinct from the aerobic dicarboxylate transport system (Det), J. Bacteriol. 176, 6470-6478.
29. Hayaishi, O. (1955) Enzymatic decarboxylation of malonic acid, J. Biol. Chem. 215, 125-136.
30. + pump and evidence for their function, Eur. J. Biochem. 245, 103-115.
31. Hoenke, S., Schmid, M. & Dimroth, P. (1997) Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli, Eur. J. Biochem. 246, 530-538.
32. Byun, H. S. & Kim, Y. S. (1995) CoA transferase and malonyl-CoA decarboxylase activity of malonate decarboxylase from Acinotobacter calcoaceticus, J. Biochem. Mol. Biol. 28, 107-111.
33. Koo, J. H., Jung, S. B., Byun, H. S. & Kim, Y. S. (1997) Cloning and sequencing of genes encoding malonate decarboxylase in Acinetobacter calcoaceticus, Biochim. Biophys. Acta 1354, 49-54.
34. Engel, P., Kramer, P. & Unden, G. (1992) Anaerobic fumarate transport in Escherichia coli by an fnr-dependent dicarboxylate uptake system which is different from the aerobic dicarboxylate uptake system, J. Bacteriol. 174, 5533-5539.
35. Glenn, A. M. & Dilworth, M. J. (1981) Oxidation of substrates by isolated bacteroids and free-living cells of Rhizobium leguminosarum 3841, J. Gen. Bacteriol. 126, 243-247.
36. Walshaw, D. L., Wilkinson, A., Mundy, M., Smith, M. & Poole, P. S. (1997) Regulation of the TCA cycle and the general amino acid permease by overflow metabolism in Rhizobium leguminosarum, Microbiology 143, 2209-2221.