1887

Abstract

Maltose metabolism in involves the conversion of -glucose 1-phosphate to glucose 6-phosphate, a reaction which is reversibly catalysed by a maltose-inducible and glucose-repressible -phosphoglucomutase (-PGM). The gene encoding -PGM () was cloned from a genomic library of using antibodies. The nucleotide sequence of a 5695 bp fragment was determined and six ORFs, including the gene, were found. The gene expressed a polypeptide with a calculated molecular mass of 24210 Da, which is in agreement with the molecular mass of the purified -PGM (25 kDa). A short sequence at the N-terminus was found to be similar to known metal-binding domains. The expression of -PGM in was found to be induced also by trehalose and sucrose, and repressed by lactose in the growth medium. This indicates that -PGM does not serve solely to degrade maltose, but that it is also involved in the metabolism of other carbohydrates. The specific activity of a-PGM during fermentation was dependent on the maltose concentration in the medium. The maximum specific activity of -PGM increased by a factor of 4.6, and the specific growth rate by a factor of 7, when the maltose concentration was raised from 0.8 to 11.0 g I. Furthermore, a higher amount of lactate produced relative to formate, acetate and ethanol was observed when the initial maltose concentration in the medium was increased. The specific activity of -PGM responded similarly to -PGM, but the magnitude of the response was lower. Preferential sugar utilization and a- and -PGM suppression was observed when was grown on the substrate combinations glucose and maltose, or lactose and maltose; maltose was the least-preferred sugar. In contrast, galactose and maltose were utilized concurrently and both PGM activities were high throughout the fermentation.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-143-3-855
1997-03-01
2024-11-09
Loading full text...

Full text loading...

/deliver/fulltext/micro/143/3/mic-143-3-855.html?itemId=/content/journal/micro/10.1099/00221287-143-3-855&mimeType=html&fmt=ahah

References

  1. Ben-Zvi R., Schramm M. 1961; A phosphoglucomutase specific for β-glucose 1-phosphate.. J Biol Chem 236:2186–2189
    [Google Scholar]
  2. Bone R., Frank L., Springer J.P., Atack J.R. 1994; Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis.. Biochemistry 33:9468–9476
    [Google Scholar]
  3. Bradford M.M. 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
    [Google Scholar]
  4. Brautaset T., Standal R., Fjaervik E., Valla S. 1994; Nucleotide sequence and expression analysis of the Acetobacter xylinum phosphoglucomutase gene.. Microbiology 140:1183–1188
    [Google Scholar]
  5. Citti J.E., Sandine W.E., Elliker P.R. 1966; Lactose and maltose uptake by Streptococcus lactis. . J Dairy Sci 50:485–488
    [Google Scholar]
  6. Dai J.B., Liu Y., Ray W.J., Konno M. 1992; The crystal structure of muscle phosphoglucomutase refined at 2-7-angstrom resolution.. J Biol Chem 267:6322–6337
    [Google Scholar]
  7. De Vos W.M., Boerrigter I., van Rooyer R.J., Reiche B., Hengstenberg W. 1990; Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis. . J Biol Chem 265:22554–22560
    [Google Scholar]
  8. Fitting C., Doudoroff M. 1952; Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis. . J Biol Chem 199:153–163
    [Google Scholar]
  9. Frischauf A.M., Lehrach H., Poustka A., Murray N. 1983; Lambda replacement vectors carrying polylinker sequences.. J Mol Biol 170:827–842
    [Google Scholar]
  10. Laemmli U.K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4.. Nature 227:680–685
    [Google Scholar]
  11. Ludwig W., Seewaldt E., Kilpper-Bölz R., Schleifer K.H., Magrum L., Woese C.R., Fox G.E., Stackebrandt E. 1985; The phylogenetic position of Streptococcus and Enterococcus. . J Gen Microbiol 131:543–551
    [Google Scholar]
  12. Magasanik B., Neidhardt F.C. 1987; Regulation of carbon and nitrogen utilization.. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology pp. 1318–1325 Edited by Neidhardt F. C., Ingraham J. L., Brooks Low K., Magasanik B., Schaechter M., Umbarger H. E. Washington, DC: American Society for Microbiology;
    [Google Scholar]
  13. Maréchal , Belocopitow E. 1974; Metabolism of trehalose in Euglena gracilis. . Eur J Biochem 42:45–50
    [Google Scholar]
  14. Maréchal L.R., Oliver G., Veiga L.A., de Ruiz Holgado A.A.P. 1984; Partial purification and some properties of β- phosphoglucomutase from Lactobacillus brevis. . Arch Biochem Biophys 228:592–599
    [Google Scholar]
  15. Minami Y., Emori Y., Kawasaki H., Suzuki K. 1987; E-F hand structure-domain of calcium-activated neutral protease (CANP) can bind Ca2+ ions.. J Biochem 101:889–895
    [Google Scholar]
  16. Moustafa H.H., Collins E.B. 1968; Role of galactose or glucose 1-phosphate in preventing the lysis of Streptococcus diacetilactis. . J Bacteriol 95:592–602
    [Google Scholar]
  17. Oh D., Hopper J.E. 1990; Transcription of a yeast phospho-glucomutase isozyme gene is galactose inducible and glucose repressible.. Mol Cell Biol 10:1415–1422
    [Google Scholar]
  18. Qian N., Stanley G.A., Hahn-Högerdal B., Rödström P. 1994; Purification and characterization of two phosphoglucomutases from Lactococcus lactis subsp.lactis and their regulation in maltose and glucose utilizing cells.. J Bacteriol 176:5304–5311
    [Google Scholar]
  19. Ray W.J. Jr Peck E.J. Jr 1972; Phosphomutases.. In The Enzymes, 3rd edn,. 6 pp. 407–458 Edited by Boyer P. D. New York: Academic Press;
    [Google Scholar]
  20. Saier M.H. Jr Chauvaux S., Cook M.G., Deutscher J., Paulsen I.T., Reizer J., Ye J. 1996; Catabolite repression and inducer control in Gram-positive bacteria.. Microbiology 142:217–230
    [Google Scholar]
  21. Sambrook J., Fritsch E.F., Maniatis T. 1989 Molecular Cloning: a Laboratory Manual, 2nd edn.. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  22. Sanger F., Nicklen S., Coulson A.R. 1977; DNA sequencing with chain-terminating inhibitors.. Proc Natl Acad Sci USA 745463–5467
    [Google Scholar]
  23. Sjöberg A., Hahn-Hägerdal B. 1989; β-Glucose-l-phosphate, a possible mediator for polysaccharide formation in maltose- assimilating Lactococcus lactis. . Appl Environ Microbiol 55:1549–1554
    [Google Scholar]
  24. Sjöberg A., Persson I., Quednau M., Hahn-Hägerdal B. 1995; The influence of limiting and non-limiting growth conditions on glucose and maltose metabolism in Lactococcus lactis ssp.lactis strains.. Appl Microbiol Biotechnol 42:931–938
    [Google Scholar]
  25. Sorimachi H., Ohmi S., Emori Y., Kawasaki H., Saido T.C., Ohno S., Minami Y., Suzuki K. 1990; A novel member of the calcium-dependent cysteine protease family.. Biol Chem Hoppe- Seyler (Suppl.) 371:171–176
    [Google Scholar]
  26. Terzaghi B.E., Sandine W.E. 1975; Improved medium for lactic streptococci and their bacteriophages.. Appl Environ Microbiol 29:807–813
    [Google Scholar]
  27. Thomas T.D., Turner K.W., Crow V.L. 1980; Galactose fermentation by Streptococcus lactis and Streptococcus cremoris: pathways, products, and regulation.. J Bacteriol 144:672–682
    [Google Scholar]
  28. Thompson J. 1980; Galactose transport systems in Streptococcus lactis. . J Bacteriol 144:683–691
    [Google Scholar]
  29. Thompson J. 1987; Regulation of sugar transport and metab-olism in lactic acid bacteria.. FEMS Microbiol Rev 46:221–231
    [Google Scholar]
  30. Thompson J., Saier M.H. 1981; Regulation of methyl-β-d- thiogalactopyranoside-6-phosphate accumulation in Streptococcus lactis by exclusion and expulsion mechanisms.. J Bacteriol 146:885–894
    [Google Scholar]
  31. Thompson J.D., Turner K.W., Thomas T.D. 1978; Catabolite inhibition and sequential metabolism of sugars by Streptococcus lactis. . J Bacteriol 133:1163–1174
    [Google Scholar]
  32. Vargas M.A., Orozco E. 1993; Entamoeba histolytica: changes in the zymodeme of cloned nonpathogenic trophozoites cultured under different conditions.. Parasitol Res 79:353–356
    [Google Scholar]
  33. Vieira J.D., Messing J. 1982; The pUC plasmids, an M13mp7- derived system for insertion mutagenesis and sequencing with synthetic universal primers.. Gene 19:259–268
    [Google Scholar]
/content/journal/micro/10.1099/00221287-143-3-855
Loading
/content/journal/micro/10.1099/00221287-143-3-855
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error