Phospho-β-glucosidase from Fusobacterium mortiferum: Purification, cloning, and inactivation by 6-phosphoglucono-δ-lactone

Journal of Bacteriology

Volumn 179, Issue 5, 1997, Pages 1636-1645

  Thompson, John ^a   Robrish, Stanley A ^a   Bouma, Carolyn L ^a   Freedberg, Darón I ^a   Folk, J E ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSIDASE;

ARTICLE; ENZYME CHEMISTRY; ENZYME INACTIVATION; ENZYME PURIFICATION; FUSOBACTERIUM; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL;

ESCHERICHIA COLI; FUSOBACTERIUM MORTIFERUM;

EID: 0031038989     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.5.1636-1645.1997     Document Type: Article

References (53)

1. Altschul, S. F., W. Gish, W. Miller, E. W. Myers, and D. J. Lipman. 1990. Basic local alignment search tool. J. Mol. Biol. 215:403-410.
2. Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. A. Smith, J. G. Seidman, and K. Struhl (ed.). 1992. Current protocols in molecular biology. John Wiley & Sons, Inc., New York.
3. Baker, P. J., K. L. Britton, D. W. Rice, A. Rob, and T. J. Stillman. 1992. Structural consequences of sequence patterns in the fingerprint of the nucleotide binding fold. Implications for nucleotide specificity. J. Mol. Biol. 228:662-671.
4. Beutler, E., and W. Kuhl. 1986. Characteristics and significance of the reverse glucose-6-phosphate dehydrogenase reaction. J. Lab. Clin. Med. 107: 502-507.
5. Brendel, V., and E. N. Trifonov. 1984. A computer algorithm for testing potential prokaryotic terminators. Nucleic Acids Res. 12:4411-4427.
6. El Hassouni, M., B. Henrissat, M. Chippaux, and F. Barras. 1992. Nucleotide sequences of the arb genes, which control β-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new β-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans. J. Bacteriol. 174:765-777.
7. González-Candelas, L., D. Ramón, and J. Polaina. 1990. Sequences and homology analysis of two genes encoding β-glucosidases from Bacillus polymyxa. Gene 95:31-38.
8. Gräbnitz, F., M. Seiss, K. P. Rücknagel, and W. L. Staudenbauer. 1991. Structure of the β-glucosidase gene bglA of Clostridium thermocellum. Sequence analysis reveals a superfamily of cellulases and β-glycosidases including human lactase/phlorizin hydrolase. Eur. J. Biochem. 200:301-309.
9. Hackert, M. L., and R. A. Jacobson. 1971. The crystal and molecular structure of D-glucono-(1,5)-lactone. Acta Cryst. 27:203-209.
10. Hall, B. G., and L. Xu. 1992. Nucleotide sequence, function, activation, and evolution of the cryptic asc operon of Escherichia coli K12. Mol. Biol. Evol. 9:688-706.
11. Hengstenberg, W., D. Kohlbrecher, E. Witt, R. Kruse, I. Christiansen, D. Peters, R. P. von Strandmann, P. Städtler, B. Koch, and H.-R. Kalbitzer. 1993. Structure and function of the phosphotransferase system and of 6-phospho-β-glycosidases in Gram-positive bacteria. FEMS Microbiol. Rev. 12:149-164.
12. Henrissat, B., and A. Bairoch. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293:781-788.
13. Henrissat, B., I. Callebaut, S. Fabrega, P. Lehn, J.-P. Mornon, and G. Davies. 1995. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. USA 92:7090-7094.
14. Hofstad, T. 1981. The genus Fusobacterium, p. 1464-1474. In M. P. Starr, H. Stolp, H. G. Trüper, A. Balows, and H. G. Schlegel (ed.), The prokaryotes. Vol. II. A handbook on habitats, isolation, and identification of bacteria. Springer-Verlag, Berlin.
15. Innis, M. A. 1990. PCR protocols: a guide to methods and applications. Academic Press, New York.
16. Kundig, W., S. Ghosh, and S. Roseman. 1964. Phosphate bound to histidine in a protein as an intermediate in a novel phospho-transferase system. Proc. Natl. Acad. Sci. USA 52:1067-1074.
17. Lalégerie, P., G. Legler, and J. M. Yon. 1982. The use of inhibitors in the study of glycosidases. Biochimie 64:977-1000.
18. Leaback, D. H. 1968. On the inhibition of β-N-acetyl-D-glucosaminidase by 2-acetamido-2-deoxy-D-glucono-(1,5)-lactone. Biochem. Biophys. Res. Commun. 32:1025-1030.
19. Leaback, D. H., and P. G. Walker. 1961. Studies on glucosaminidase. 4. The fluorimetric assay of N-acetyl-β-glucosaminidase. Biochem. J. 78:151-156.
20. Legler, G. 1990. Glycoside hydrolases: mechanistic information from studies with reversible and irreversible inhibitors. Adv. Carbohydr. Chem. Biochem. 48:319-384.
21. Levvy, G. A., A. J. Hay, and J. Conchie. 1964. Inhibition of glycosidases by aldonolactones of corresponding configuration. 4. Inhibitors of mannosidase and glucosidase. Biochem. J. 91:378-384.
22. Meadow, N. D., D. K. Fox, and S. Roseman. 1990. The bacterial phosphoenolpyruvate: glycose phosphotransferase system. Annu. Rev. Biochem. 59:497-542.
23. AL, p. 631-637. In N. R. Krieg, and J. G. Holt (ed.), Bergey's manual of systematic bacteriology, Vol. 1. Williams & Wilkins, Baltimore.
24. Palmer, R. E., and R. L. Anderson. 1972. Cellobiose metabolism in Aerobacter aerogenes. II. Phosphorylation of cellobiose with adenosine 5′- triphosphate by a β-glucosidase. J. Biol. Chem. 247:3415-3419.
25. Palmer, R. E., and R. L. Anderson. 1972. Cellobiose metabolism in Aerobacter aerogenes. III. Cleavage of cellobiose monophosphate by a phospho- β-glucosidase. J. Biol. Chem. 247:3420-3423.
26. Parker, L. L., and B. G. Hall. 1990. Characterization and nucleotide sequence of the cryptic cel operon of Escherichia coli K12. Genetics 124:455- 471.
27. Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
28. Postma, P. W., J. W. Lengeler, and G. R. Jacobson. 1993. Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57:543-594.
29. Reizer, J., M. H. Saier, Jr., J. Deutscher, F. Grenier, J. Thompson, and W. Hengstenberg. 1988. The phosphoenolpyruvate: sugar phosphotransferase system in Gram-positive bacteria: properties, mechanism, and regulation. Crit. Rev. Microbiol. 15:297-338.
30. Robrish, S. A., H. M. Fales, C. Gentry-Weeks, and J. Thompson. 1994. Phosphoenolpyruvate-dependent maltose-phosphotransferase activity in Fusobacterium mortiferum ATCC 25557: specificity, inducibility, and product analysis. J. Bacteriol. 176:3250-3256.
31. Robrish, S. A., C. Oliver, and J. Thompson. 1991. Sugar metabolism by Fusobacteria: regulation of transport, phosphorylation, and polymer formation by Fusobacterium mortiferum ATCC 25557. Infect. Immun. 59:4547- 4554.
32. Robrish, S. A., and J. Thompson. 1990. Regulation of fructose metabolism and polymer synthesis by Fusobacterium nucleatum ATCC 10953. J. Bacteriol. 172:5714-5723.
33. Rojas, A., L. I. Arola, and A. Romeu. 1995. β-Glucosidase families revealed by computer analysis of protein sequences. Biochem. Mol. Biol. Int. 35:1223- 1231.
34. Roseman, S. 1989. Sialic acid, serendipity, and sugar transport: discovery of the bacterial phosphotransferase system. FEMS Microbiol. Rev. 63:3-12.
35. Saier, M. H., Jr., and J. Reizer. 1992. Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol. 174:1433-1438.
36. Schnetz, K., C. Toloczyki, and B. Rak. 1987. β-Glucoside (bgl) operon of Escherichia coli K-12: nucleotide sequence, genetic organization, and possible evolutionary relationship to regulatory components of two Bacillus subtilis genes. J. Bacteriol. 169:2579-2590.
37. m enzyme. Biochem. Biophys. Res. Commun. 71:1313-1318.
38. Scrutton, N. S., A. Berry, and R. N. Perham. 1990. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343:38-43.
39. Silhavy, T. J., M. L. Berman, and L. W. Enquist. 1984. Experiments with gene fusions. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
40. Sinnott, M. L. 1987. Glycosyl group transfer, p. 259-297. In M. I. Page, and A. Williams (ed.), Enzyme mechanisms. The Royal Society of Chemistry, London.
41. Sinnott, M. L. 1990. Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90:1171-1202.
42. Tanaka, A., M. Ito, and K. Hiromi. 1986. Equilibrium and kinetic studies of binding of gluconolactone to almond β-glucosidase in the absence and presence of glucose. J. Biochem.100:1379-1385.
43. Thompson, J. 1987. Sugar transport in the lactic acid bacteria, p. 13-38. In J. Reizer and A. Peterkofsky (ed.), Sugar transport and metabolism in gram- positive bacteria. Ellis Horwood, Chichester, Great Britain.
44. Thompson, J., C. R. Gentry-Weeks, N. Y. Nguyen, J. E. Folk, and S. A. Robrish. 1995. Purification from Fitsobacterium mortiferum ATCC 25557 of a 6-phosphoryl-O-α-D-glucopyranosyl:6-phosphoglucohydrolase that hydrolyzes maltose 6-phosphateand related phospho-α-D-glucosides. J. Bacteriol. 177:2505-2512.
45. Thompson, J., N. Y. Nguyen, and S. A. Robrish. 1992. Sucrose fermentation by Fusobacterium moniferum ATCC 25557: transport, catabolism, and products. J. Bacteriol. 174:3227-3235.
46. Wang, Q., and S. G. Withers. 1995. Substrate-assisted catalysis in glycosidases. J. Am. Chem. Soc. 117:10137-10138.
47. Wierenga, R. K., P. Terpstra, and W. G. J. Hol. 1986. Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187:101-107.
48. Wiesmann, C., G. Beste, W. Hengstenberg, and G. E. Schulz. 1995. The three-dimensional structure of 6-phospho-β-galactosidase from Lactococcus lactis. Structure 3:961-968.
49. Wilson, G., and C. F. Fox. 1974. The β-glucoside system of Escherichia coli. IV. Purification and properties of phospho-β-glucosidases A and B. J. Biol. Chem. 249:5586-5598.
50. Withers, S. G., K. Rupitz, D. Trimbur, and R. A. J. Warren. 1992. Mechanistic consequences of mutation of the active site nucleophile Glu 358 in Agrobacterium β-glucosidase. Biochemistry 31:9979-9985.
51. Withers, S. G., R. A. J. Warren, I. P. Street, K. Rupitz, J. B. Kemptun, and R. Aebersold. 1990. Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glycosidase. J. Am. Chem. Soc. 112:5887-5889.
52. Witt, E., R. Frank, and W. Hengstenberg. 1993. 6-Phospho-β-galactosidases of Gram-positive and 6-phospho-β-glucosidase B of Gram-negative bacteria: comparison of structure and function by kinetic and immunological methods and mutagenesis of the lacG gene of Staphylococcus aureus. Protein Eng. 6:913-920.
53. Zhang, J., and A. Aronson. 1994. A Bacillus subtilis bglA gene encoding phospho-β-glucosidase is inducible and closely linked to a NADH dehydrogenase-encoding gene. Gene 140:85-90.