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Properties of isocitrate lyase fromEscherichia coli K12 grown on acetate or glycolate

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Abstract

Properties of isocitrate lyase fromEscherichia coli, the first enzyme of the glyoxylate bypass, have been compared from cells grown on either acetate or glycolate as the sole carbon source. Michaelis constants for isocitrate, isoelectric points, native and subunit molecular weights, antigenic properties, peptide mapping with V-8 or trypsin, and several other properties were examined. Our data suggest that only one isocitrate lyase form exists inE. coli regardless of carbon source used for growth.

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Literature Cited

  1. Bellion E, Woodson J (1975) Two distinct isocitrate lyases from aPseudomonas species. J Bacteriol 122:557–564

    PubMed  Google Scholar 

  2. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248–254

    PubMed  Google Scholar 

  3. Cioni M, Pinzauti G, Vanni P (1981) Comparative biochemistry of the glyoxylate cycle. Comp Biochem Physiol 70B:1–26

    Google Scholar 

  4. Cleveland DW, Fischer SG, Kirschner MW, Laemmli UK (1977) Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem 252:1102–1106

    PubMed  Google Scholar 

  5. Conder MJ, Ko Y-H, McFadden BA (1988) Purification of isocitrate lyase fromEscherichia coli and watermelon using fast protein liquid chromatography. Prep Biochem 18:431–442

    PubMed  Google Scholar 

  6. Dixon GH, Kornberg HL (1959) Assay methods for key enzymes of the glyoxylate cycle. Biochem J 72:3P

    Google Scholar 

  7. Falmagne P, Vanderwinkel E, Wiame JM (1965) Mise en evidence de deux malate synthases chezEscherichia coli. Biochim Biophys Acta 99:246–258

    PubMed  Google Scholar 

  8. Harrop LC, Kornberg HL (1966) The role of isocitrate lyase in the metabolism of algae. Proc R Soc London 166:11–29

    Google Scholar 

  9. Hillier S, Charnetzky WT (1981) Glyoxylate bypass enzymes inYersinia species and multiple forms of isocitrate lyase inYersinia pestis. J. Bacteriol 145:452–458

    PubMed  Google Scholar 

  10. Kornberg HL (1966) Anaplerotic sequences and their role in metabolism. In: Campbell PN, Greville GD (eds) Essays in biochemistry, vol. 2. London, New York: Academic Press, pp 1–29

    Google Scholar 

  11. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685

    PubMed  Google Scholar 

  12. Lineweaver H, Burk D (1934) The determination of enzyme dissociation constants. J Amer Chem Soc 56:658–666

    Google Scholar 

  13. Robertson EF, Reeves HC (1987) Purification and characterization of isocitrate lyase fromEscherichia coli. Curr Microbiol 14:347–350

    Google Scholar 

  14. Robertson EF, Hoyt JC, Reeves HC (1987) In vitro phosphorylation ofEscherichia coli isocitrate lyase. Curr Microbiol 15:103–105

    Google Scholar 

  15. Robertson EF, Dannelly HK, Malloy PJ, Reeves HC (1987) Rapid isoelectric focusing in a vertical polyacrylamide minigel system. Anal Biochem 167:290–294

    PubMed  Google Scholar 

  16. Robertson EF, Hoyt JC, Reeves HC (1988) Evidence of histidine phosphorylation in isocitrate lyase fromEscherichia coli. J Biol Chem 263:2477–2482

    PubMed  Google Scholar 

  17. Sjogren RE, Romano AH (1967) Evidence for multiple forms of isocitrate lyase inNeurospora crassa. J Bacteriol 93:1638–1643

    PubMed  Google Scholar 

  18. Vanderwinkel E, De Vlieghere M (1968) Physiologie et genetique de l'isocitratase et des malate synthases chezEscherichia coli. Eur J Biochem 5:81–90

    PubMed  Google Scholar 

  19. Wegener WS, Schell JE, Romano AH (1967) Control of malate synthase formation inRhizopus nigricans. J Bacteriol 94:1951–1956

    PubMed  Google Scholar 

  20. Zarembinski CM, Hoyt JC, Reeves HC (1988) Comparison of isocitrate lyase fromEscherichia coli K12 grown on different carbon sources. J Cell Biol 107:187a

    Google Scholar 

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Zarembinski, C.M., Hoyt, J.C. & Reeves, H.C. Properties of isocitrate lyase fromEscherichia coli K12 grown on acetate or glycolate. Current Microbiology 22, 65–68 (1991). https://doi.org/10.1007/BF02106215

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