PubMedCrossRef 46 Hogema BM, Arents JC, Bader R, Eijkemans K, Yo

PubMedCrossRef 46. Hogema BM, Arents JC, Bader R, Eijkemans K, Yoshida H, Takahashi H, Aiba H, Postma PW: Inducer exclusion in Escherichia coli by non-PTS substrates: the role of the PEP to pyruvate ratio in determining the phosphorylation state of enzyme IIA Glc . Mol Microbiol 1998, 30:487–498.PubMedCrossRef 47. Haest CW, de Gier J, van Deenen LL: Changes in the chemical and barrier properties of the membrane lipids of E. coli by variation of the temperature of growth. Chem Phys Lipids 1969, 3:413–417.PubMedCrossRef see more 48. Davies DG, Parsek MR, Pearson JP, Iglewski BH, Costerton JW, Selleckchem P005091 Greenberg EP: The involvement of cell-to-cell signals in the development of a bacterial biofilm. Science 1998, 280:295–298.PubMedCrossRef

49. Otto M: Quorum-sensing

control in Staphylococci – a target for antimicrobial drug therapy? FEMS Microbiol Lett 2004, 241:135–141.PubMedCrossRef 50. Datsenko KA, Wanner BL: One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 2000, 97:6640–6645.PubMedCrossRef 51. Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H: Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2006, 2:2006.0008.PubMedCrossRef 52. Walters MC III, Roe F, Bugnicourt A, Franklin MJ, Stewart PS: Contributions of antibiotic penetration, oxygen limitation, and low metabolic activity to tolerance of Pseudomonas aeruginosa biofilms to ciprofloxacin Amylase and tobramycin. Antimicrob Agents Chemother 2003, 47:317–323.PubMedCrossRef 53. Hamilton M: The Biofilm Laboratory Step-By-Step Ganetespib clinical trial Protocols for Experimental Design, Analysis, and Data Interpretation. Edited by: Hamilton M, Heersink J, Buckingham-Meyer K, Goeres D. Cytergy Publishing, Bozeman MT; 2003. 54. Herigstad B, Hamilton M, Heersink J: How to optimize the drop plate method for enumerating bacteria.

J Microbiol Methods 2001, 44:121–129.PubMedCrossRef Authors’ contributions Conception and design of experiment: TRZ, RPC. Acquisition of data: TRZ, HB, JLR, LJT. Analysis and interpretation of data: TRZ, PSS, RPC. Drafting the manuscript: PSS, RPC. Revising the manuscript critically for intellectual content: TRZ, HB, PSS, RPC. Final approval of published version: TRZ, HB, JLR, LJT, PSS, RPC.”
“Background Carbonic anhydrases (CAs, EC 4.2.1.1) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide to bicarbonate (CO2 + H2O ↔ HCO3 – + H+). This simple interconversion of a membrane-permeable gas substrate into a membrane-impermeable ionic product is vital to many important biological functions; such enzymes are thus widely distributed in nature. On the basis of differences in amino acid sequence and structure, carbonic anhydrases are divided into five distinct, evolutionarily unrelated gene families: α, β, γ and the recently discovered δ and ζ [1–4].

Comments are closed.