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Novel NADP-linked isocitrate dehydrogenase present in peroxisomes of n-alkane-utilizing yeast, Candida tropicalis: comparison with mitochondrial NAD-linked isocitrate dehydrogenase

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Abstract

Peroxisomal NADP-linked isocitrate dehydrogenase (Ps-NADP-IDH) was purified for the first time from Candida tropicalis cells grown on n-alkane as a carbon source, which was effective in proliferation of peroxisomes. The properties of Ps-NADP-IDH were compared with those of mitochondrial NAD-linked isocitrate dehydrogenase (Mt-NAD-IDH) purified from the cells grown on acetate, in which peroxisomes did not proliferate. Ps-NADP-IDH was a homodimer of identical subunits (45 kDa), while Mt-NAD-IDH was suggested to be a heterooctamer composed of two types of subunits with different molecular masses (41 and 38 kDa). Kinetic studies revealed that Ps-NADP-IDH gave Michaelis-Menten saturation curves against isocitrate and NADP concentrations, whereas Mt-NAD-IDH was an allosteric enzyme regulated by ATP, AMP, and citrate. Inhibition by 2-oxoglutarate, a precursor of glutamate, was observed only for Ps-NADP-IDH. Both enzymes were inhibited by concomitant addition of oxalacetate and glyoxylate. The function of Ps-NADP-IDH seems to be completely discriminated from that of Mt-NAD-IDH as reflected by their distinct subcellular localizations. Furthermore, the properties of Ps-NADP-IDH were also compared with those of other mitochondrial and cytosolic IDHs from sources reported previously.

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References

  • Bernofsky C, Utter MF (1966) Mitochondrial isocitrate dehydrogenase from yeast. J Biol Chem 241:5461–5466

    Article  CAS  Google Scholar 

  • Borthwick AC, Holms WH, Nimmo HG (1984) Isolation of active and inactive forms of isocitrate dehydrogenase from Escherichia coli ML308. Eur J Biochem 141:393–400

    Article  CAS  Google Scholar 

  • Carlier MF, Pantaloni D (1973) NADP-Linked isocitrate dehydrogenase from beef liver-Purification, quaternary structure and catalytic activity. Eur J Biochem 37:341–354

    Article  CAS  Google Scholar 

  • Chen RF, Plaut GWE (1963) Activation and inhibition of DPN-linked isocitrate dehydrogenase of heart by certain nucleotides. Biochemistry 2:1023–1032

    Article  CAS  Google Scholar 

  • Cleveland DW, Fischer SG, Kirscher MW, Laemmli UK (1977) Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem 252:1101–1106

    Article  Google Scholar 

  • Colman RF (1968) Effect of modification of a methionyl residue on the kinetic and molecular properties of isocitrate dehydrogenase. J Biol Chem 243:2454–2464

    Article  CAS  Google Scholar 

  • Eguchi H, Wakagi T, Oshima T (1989) A highly stable NADP-dependent isocitrate dehydrogenase from Thermus thermophilus HB8: purification and general properties. Biochim Biophys Acta 990:133–137

    Article  CAS  Google Scholar 

  • Ehrlich RS, Colman RF (1990) Conformation on the coenzymes and the allosteric activator, ADP, bound to NAD+-dependent isocitrate dehydrogenase from pig heart. Biochemistry 29:5179–5187

    Article  CAS  Google Scholar 

  • Fatania H, Al-Nassar KE, Sidhan V (1993) Purification and partial characterisation of NADP+-linked isocitrate dehydrogenase from rat liver cytosol. FEBS Lett 1:57–60

    Article  Google Scholar 

  • Fukui S, Tanaka A (1983) Peroxisomes of alkane-utilizing yeasts —Metabolic functions and practical aspects. Acta Biotechnol 3:327–337

    Article  CAS  Google Scholar 

  • Gabriel JL, Plaut GWE (1991) Kinetic regulation of yeast NAD-specific isocitrate dehydrogenase by citrate. Biochemistry 30:2594–2599

    Article  CAS  Google Scholar 

  • Haselbeck RJ, McAlister-Henn L (1991) Isolation, nucleotide sequence, and disruption of the Saccharomyces cerevisiae gene encoding mitochondrial NADP(H)-specific isocitrate dehydrogenase. J Biol Chem 266:2339–2345

    Article  CAS  Google Scholar 

  • Haselbeck RJ, McAlister-Henn L, (1993) Function and expression of yeast mitochondrial NAD-and NADP-specific isocitrate dehydrogenases. J Biol Chem 268:12116–12122

    Article  CAS  Google Scholar 

  • Haselbeck RJ, Colman RF, McAlister-Henn L (1992) Isolation and sequence of a cDNA encoding porcine mitochondrial NADP-specific isocitrate dehydrogenase. Biochemistry 31:6219–6223

    Article  CAS  Google Scholar 

  • Hirai M, Shiotani T, Tanaka A, Fukui S (1976) Intracellular localization of several enzymes in Candida tropicalis grown on different carbon sources. Agric Biol Chem 40:1979–1985

    CAS  Google Scholar 

  • Huang Y-C, Colman RF (1990) Subunit location and sequences of the cysteinyl peptides of pig heart NAD-dependent isocitrate dehydrogenase. Biochemistry 29:8266–8273

    Article  CAS  Google Scholar 

  • Illingworth JA, Tipton KF (1970) Purification and properties of the nicotinamide-adenine dinucleotide phosphate-dependent isocitrate dehydrogenase from pig liver cytoplasm. Biochem J 118:253–258

    Article  CAS  Google Scholar 

  • Kawamoto S, Tanaka A, Yamamura M, Teranishi Y, Fukui S, Osumi M (1977) Microbody of n-alkane-grown yeast. Enzyme localization in the isolated microbody. Arch Microbiol 112: 1–8

    Article  CAS  Google Scholar 

  • Keys DA, McAlister-Henn L (1990) Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae. J Bacteriol 172:4280–4287

    Article  CAS  Google Scholar 

  • Leyland ML, Kelly D (1991) Purification and characterization of a monomeric isocitrate dehydrogenase with dual coenzyme specificity from the photosynthetic bacterium Rhodomicrobium vannielii. Eur J Biochem 202:85–93

    Article  CAS  Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275

    Article  CAS  Google Scholar 

  • Macfarlane N, Mathews B, Dalziel K (1977) The purification and properties of NADP-dependent isocitrate dehydrogenase from ox-heart mitochondria. Eur J Biochem 74:553–559

    Article  CAS  Google Scholar 

  • Moyle J, Mitchell P (1973) The proton-translocating nicotinamideadenine dinucleotide (phosphate) transhydrogenase of rat liver mitochondria. Biochem J 132:571–585

    Article  CAS  Google Scholar 

  • Nabeshima S, Ishiyama S, Tanaka A, Fukui S (1977) Partial purification and some kinetic properties of NAD-linked and NADP-linked isocitrate dehydrogenases from Candida tropicalis. Agric Biol Chem 41:509–516

    CAS  Google Scholar 

  • Nakayama T (1981) Denkieidou no subete (Japanese). Gekkan Medical Technology, Tokyo, Japan, pp 174–181

    Google Scholar 

  • Plaut GWE, Aogaichi T (1968) Purification and properties of diphosphopyridine nucleotide-linked isocitrate dehydrogenase of mammalian liver. J Biol Chem 243:5572–5583

    Article  CAS  Google Scholar 

  • Uchida M, Ueda M, Matsuki T, Okada H, Tanaka A, Fukui S (1986) Properties of isocitrate lyase from an alkane-utilizable yeast, Candida tropicalis. Agric Biol Chem 50:127–134

    CAS  Google Scholar 

  • Ueda M, Okada H, Tanaka A, Osumi M, Fukui S (1983) Induction and subcellular localization of enzymes participating in propionate metabolism in Candida tropicalis. Arch Microbiol 136:169–176

    Article  CAS  Google Scholar 

  • Ueda M, Tanaka A, Fukui S (1984) Characterization of peroxisomal and mitochondrial carnitine acetyltransferases purified from alkane-grown Candida tropicalis. Eur J Biochem 138:445–449

    Article  CAS  Google Scholar 

  • Ueda M, Yamanoi K, Morikawa T, Okada H, Tanaka A (1985) Peroxisomal localization of enzymes related to fatty acid \-oxidation in an n-alkane-grown yeast, Candida tropicalis. Agric Biol Chem 49:1821–1828

    CAS  Google Scholar 

  • Vasquez B, Reeves HC (1979) NADP-specific isocitrate dehydrogenase of Escherichia coli-IV. Purification by chromatography on affi-gel blue. Biochim Biophys Acta 578:31–40

    Article  CAS  Google Scholar 

  • Westwood JT, Clos J, Wu C (1991) Stress-induced oligomerization and chromosomal relocalization of heat-shock factor. Nature 353:822–827

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Laboratory of Applied Biological Chemistry, Department of Synthetic Chemistry and Biological Chemistry, Faculty of Engineering, Kyoto University, Yoshida, Sakyo-ku, 606-01, Kyoto, Japan

    Setsuko Yamamoto, Haruyuki Atomi, Mitsuyoshi Ueda & Atsuo Tanaka

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  1. Setsuko Yamamoto
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  2. Haruyuki Atomi
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  3. Mitsuyoshi Ueda
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  4. Atsuo Tanaka
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Yamamoto, S., Atomi, H., Ueda, M. et al. Novel NADP-linked isocitrate dehydrogenase present in peroxisomes of n-alkane-utilizing yeast, Candida tropicalis: comparison with mitochondrial NAD-linked isocitrate dehydrogenase. Arch. Microbiol. 163, 104–111 (1995). https://doi.org/10.1007/BF00381783

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  • DOI: https://doi.org/10.1007/BF00381783

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