Abstract
Streptococcus bovis possesses two sugar phosphate phosphatases (Pases). Pase I is a soluble enzyme that is inhibited by the membrane fractions from lactose-grown cells and is insensitive to activation by S46D HPr, an analog of HPr(ser-P) of the sugar phosphotransferase system. Pase II is a membrane-associated enzyme that can be activated 10-fold by S46D HPr, and it appears to play a role in inducer expulsion.
Full Text
The Full Text of this article is available as a PDF (160.6 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Cook G. M., Kearns D. B., Russell J. B., Reizer J., Saier M. H., Jr Regulation of the lactose phosphotransferase system of Streptococcus bovis by glucose: independence of inducer exclusion and expulsion mechanisms. Microbiology. 1995 Sep;141(Pt 9):2261–2269. doi: 10.1099/13500872-141-9-2261. [DOI] [PubMed] [Google Scholar]
- HUNGATE R. E., DOUGHERTY R. W., BRYANT M. P., CELLO R. M. Microbiological and physiological changes associated with acute indigestion in sheep. Cornell Vet. 1952 Oct;42(4):423–449. [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- London J., Hausman S. Z., Thompson J. Characterization of a membrane-regulated sugar phosphate phosphohydrolase from Lactobacillus casei. J Bacteriol. 1985 Sep;163(3):951–956. doi: 10.1128/jb.163.3.951-956.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Reizer J., Novotny M. J., Hengstenberg W., Saier M. H., Jr Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system. J Bacteriol. 1984 Oct;160(1):333–340. doi: 10.1128/jb.160.1.333-340.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Reizer J. Regulation of sugar uptake and efflux in gram-positive bacteria. FEMS Microbiol Rev. 1989 Jun;5(1-2):149–156. doi: 10.1016/0168-6445(89)90019-3. [DOI] [PubMed] [Google Scholar]
- Reizer J., Sutrina S. L., Saier M. H., Stewart G. C., Peterkofsky A., Reddy P. Mechanistic and physiological consequences of HPr(ser) phosphorylation on the activities of the phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: studies with site-specific mutants of HPr. EMBO J. 1989 Jul;8(7):2111–2120. doi: 10.1002/j.1460-2075.1989.tb03620.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Robrish S. A., Fales H. M., Gentry-Weeks C., Thompson J. Phosphoenolpyruvate-dependent maltose:phosphotransferase activity in Fusobacterium mortiferum ATCC 25557: specificity, inducibility, and product analysis. J Bacteriol. 1994 Jun;176(11):3250–3256. doi: 10.1128/jb.176.11.3250-3256.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thompson J., Chassy B. M. Intracellular hexose-6-phosphate:phosphohydrolase from Streptococcus lactis: purification, properties, and function. J Bacteriol. 1983 Oct;156(1):70–80. doi: 10.1128/jb.156.1.70-80.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ye J. J., Reizer J., Cui X., Saier M. H., Jr Inhibition of the phosphoenolpyruvate:lactose phosphotransferase system and activation of a cytoplasmic sugar-phosphate phosphatase in Lactococcus lactis by ATP-dependent metabolite-activated phosphorylation of serine 46 in the phosphocarrier protein HPr. J Biol Chem. 1994 Apr 22;269(16):11837–11844. [PubMed] [Google Scholar]
- Ye J. J., Saier M. H., Jr Purification and characterization of a small membrane-associated sugar phosphate phosphatase that is allosterically activated by HPr(Ser(P)) of the phosphotransferase system in Lactococcus lactis. J Biol Chem. 1995 Jul 14;270(28):16740–16744. doi: 10.1074/jbc.270.28.16740. [DOI] [PubMed] [Google Scholar]