In our study an initial increase of glucose was observed and then plateaued whereas insulin continued to increase up to 30 minutes following the ingestion of foods. The same glucose and insulin response prior to exercise was seen CX-6258 in vitro in De Marco et al. study when the same amount of carbohydrates was ingested [17]. This response of glucose and insulin is common since the initial increase in glucose constitutes the main stimulus for the delayed insulin increase. Several studies attempted

to alter the carbohydrate composition of a meal prior to exercise in an effort to improve performance. A number of those studies show no improvement in exercise performance [19, 22, 31–33]. Febbraio et al. [19] utilized a similar design with the one employed in this study and

found no significant differences in exercise performance. Subjects received low and high glycemic foods (1.0 g. kg-1 of body weight) 30 min prior to a 120-min submaximal exercise bout that was followed by a 30 min time trial. Total work performed EPZ015938 molecular weight during the time trial was similar between the LGI, the HGI and the control condition. These results were evident despite the fact that carbohydrate Nutlin-3a order oxidation was greater during the HGI condition. No significant differences in exercise performance were noted in two other studies by the same group [31, 32] when subjects received LGI and HGI foods (1.0 g. kg-1 of body mass) 45 min prior to submaximal exercise that was followed again by a time trial. Although

differences in glucose and insulin levels were reported following consumption of the LGI and HGI prior to exercise, there were no apparent differences in the blood metabolites during the steady state exercise. Thomas et al. [33] used four meals with different glycemic index foods (30, 36, 73 and 100) that each provided 1.0 g. kg-1 of body weight. Ergoloid The meal was consumed 1 h prior to cycling to exhaustion at 65-70% of VO2max. The results showed no significant differences in time to exhaustion between trials. No enhancement in exercise performance was found when low and high glycemic index foods were provided 3 h prior to exercise even though there was a relative shift in substrate utilization from carbohydrate to fat following the LGI meal [22]. As far as exercise performance is concerned, results from the present study coincide with those of earlier reports suggesting that although pre-exercise GI manipulation affects pre-exercise glucose and insulin levels, it does not presumably influence the rate of muscle glycogen utilization or exercise performance. Differences in glucose levels and carbohydrate and fat oxidation during steady state exercise could influence exercise performance during a subsequent short and intense exercise.

(n = 9) (B) 106 T4 phage were mixed with 1 μg purified WT OMVs, then immediately (“”0″” min), and at 5 min intervals thereafter, samples were taken and chloroform was added to disrupt the OMVs and allow reversibly bound phage to be released. The T4 activity in each sample was determined by PFU titration and compared to the PFU produced by 106 T4 (% PFU Remaining). (n = 6) (C) Negative stain electron micrograph of the T4-OMV complex (size bar = 50 nm). In order to reveal the longer-term effects of the presence of OMVs on T4 infectivity in a microenvironment, we observed the infection and reproduction

small molecule library screening of the phage in the mixture following a 1 h incubation with the titer strain. After we co-BGB324 incubated the T4 and OMVs, we added this mixture to growing cultures of the titer strain and incubated for 1 hour instead of only 5 min. This timepoint is sufficient to allow several cycles of infection and allowed us to observe whether the OMVs in the mixture have an affect beyond the initial inactivation. To use as a comparison, we first CHIR98014 purchase determined the amount of free phage (105) that produced the equivalent PFUs to the amount

of infectious phage in the mixture when it was incubated with the titer strain for only 5 min (Figure 5A, 5 min). Then we compared the amount of PFUs formed after a 60 min incubation of cells incubated with 105 T4 or with the mixture of T4 and OMVs. We found that the sample containing the mixture

of T4 and OMVs contained fewer infectious phage as compared to both the original 106 T4 as well as the 105 free T4 samples (Figure 5A, 60 min). This suggests that the addition of OMVs to T4 significantly oxyclozanide reduces the infectivity of T4 over several generations of phage infection. Finally, we used electron microscopy to determine whether complexes between T4 and OMVs could be visualized. We found many complexes between T4 and OMV (an example is shown in Figure 5C), and in these cases, T4 was in a similar orientation as was observed between T4 and bacterial cell wall [36]. These data support the model that released OMVs and vesiculation may contribute to the innate bacterial defense against outer-membrane acting stressors. Discussion Understanding how bacteria manage to survive in hostile environments has been an important step towards understanding bacterial defense and pathogenesis. As our understanding of the bacterial world has increased, so has our appreciation of the complexity of the constant interactions that occur between bacteria and their environment. These include the well-studied interactions that occur between a pathogen and the host environment, as well as the less-appreciated interactions that occur between bacteria and the general environment.

Number in parentheses is the number of species in each category cRate

of population variability for each order was calculated as the number of species that had variable responses among sites divided by the number of species that occurred at more than one site, times 100. “na” signifies that none of the species occurred at multiple sites Variability was also high among populations of species: Vistusertib solubility dmso for both endemic and introduced taxa, roughly one-third to two-thirds of the species that occurred at more than one site responded to ants differently at different sites (Tables 3, 4). This population-level variability was not dependent on which species of ant was invading. Of 195 comparisons of paired population responses, pairs CYT387 chemical structure in which both populations (of the same Saracatinib arthropod species) were invaded by Argentine ants had a nearly identical ratio of same to different responses as did pairs of populations in which one was invaded by Argentine ants and the second was invaded by big-headed ants (Argentine—Argentine pairs exhibited the same response 49.1% of the time, Argentine—big-headed pairs exhibited the same response 46.8% of the time; Chi-square = 0.100, P = 0.752, Supplementary Table 6). Discussion Oceanic island faunas are well

known for their vulnerability to extinction. Island endemic species, for example, account for over 60% of documented animal extinctions worldwide (May et al. 1995). Many of these extinctions can be attributed at least in part to impacts resulting from introductions of wholly new faunal elements, such as terrestrial mammals (Simberloff 1995; Balmford 1996). Although arthropod extinctions and their causes are much more poorly documented, it has long been suggested that species endemic to remote

oceanic archipelagos possessing few or Tideglusib no native social insects are similarly ill-equipped, due to their evolutionary isolation, to withstand the novel predatory and competitive pressures of invasive ants (e.g., Zimmerman 1970; Howarth 1985; Gillespie 1999). In the present study examining the impacts of invasive ants on arthropod species in five Hawaiian communities, provenance was strongly associated with vulnerability. Both rare and non-rare endemic species were more likely than introduced species to be less abundant or absent in invaded plots, even after adjusting for such traditionally important factors as population density, trophic role and body size, and additionally controlling for ant density and major phylogenetic effects. This result is largely in accordance with the impressions and findings of biologists going back nearly a century (Krushelnycky et al. 2005).

Disks were observed for colour change up to 60 min. β-lactamase producer strain ATCC 29213 (#1) and β-lactamase negative strain ATCC 25923 (#2), were used as positive and negative controls respectively. Antibiotic susceptibility testing – disk diffusion and E-test The standard procedure recommended by CLSI was followed [41, 42]. Briefly, inoculum was prepared by the direct colony suspension method preferred for S.

aureus. Isolated colonies from non-selective overnight BHI agar plates were used to make a saline suspension, and turbidity was adjusted equivalent to a 0.5 McFarland turbidity standard. Thereafter, the standardized inoculum was spread uniformly on a Mueller Hinton II agar plate, allowed to dry, cefazolin disk applied to the centre of the plate, and plates incubated at 35°C for 20–24 h. The zones of inhibition Fludarabine clinical trial were GDC-0994 in vivo measured and compared

against CLSI Zone Diameter Interpretive Charts, to categorize Adriamycin in vivo isolates as susceptible, intermediate or resistant. (The CLSI 2012 charts were used, which were most current at the time of the experiments [41]). S. aureus ATCC 25923 (#2) was included in each experiment as the CLSI recommended quality control strain for disk diffusion [41]. For the zone edge test comparison criteria, ATCC 29213 (#1) and ATCC 25923 (#2) were used as the CLSI recommended positive and negative controls, showing ‘sharp’ and ‘fuzzy’ inhibition zone edges respectively. For the E-test, cefoxitin or cefepime E-test strip was applied to the inoculated plate, and following incubation at 35°C for 24 h, the MIC value was read. The CLSI interpretive criteria, most current at the time of experiments, were used to categorize isolates as susceptible, intermediate or resistant [41]. S. aureus ATCC 29213 (#1) was included in each experiment as the recommended quality control for MIC determination [41]. Experiments were similarly performed

with ‘induced’ growth cultures, wherein bacteria grown in presence of penicillin disks overnight were used as ADAM7 the starting inoculum to prepare the saline suspension. The standard procedure described above was followed. Results β-LEAF assays determine β-lactamase production and assess cefazolin activity We used a panel of S. aureus comprising two ATCC strains and 25 clinical isolates (Table 1) as a model system. Isolate numbers (eg. #1, #4, etc.), rather than full names, are used to refer to isolates as per Table 1 throughout this study. ATCC strains with established β-lactamase status, β-lactamase producing strain 29213 (#1) and β-lactamase negative strain 25923 (#2) were used as positive and negative controls respectively. Cefazolin, a first generation cephalosporin, was used as the test antibiotic in these experiments. Each isolate was assayed under two conditions, with β-LEAF alone and with β-LEAF and saturating concentration of cefazolin (2500-fold higher concentration of cefazolin than β-LEAF) respectively.

Proc Natl Acad Sci U S A 2003,100(7):3677–3682.PubMedCrossRef 14. Baumler AJ, Tsolis RM, van der Crenolanib Velden AW, Stojiljkovic I, Anic S, Heffron F: Identification of a new iron regulated locus of Salmonella typhi. Gene 1996,183(1–2):207–213.PubMedCrossRef ATM Kinase Inhibitor concentration 15.

Bister B, Bischoff D, Nicholson GJ, Valdebenito M, Schneider K, Winkelmann G, Hantke K, Sussmuth RD: The structure of salmochelins: C-glucosylated enterobactins of Salmonella enterica. BioMetals 2004,17(4):471–481.PubMedCrossRef 16. Negre VL, Bonacorsi S, Schubert S, Bidet P, Nassif X, Bingen E: The siderophore receptor IroN, but not the high-pathogenicity island or the hemin receptor ChuA, contributes to the bacteremic step of Escherichia coli neonatal meningitis. Infect Immun 2004,72(2):1216–1220.PubMedCrossRef 17. Bauer RJ, Zhang L, Foxman B, Siitonen A, Jantunen ME, Saxen H, Marrs CF: Molecular epidemiology of 3 putative virulence genes for Escherichia coli urinary tract infection-usp, iha, and iroN(E. coli). J Infect Dis 2002,185(10):1521–1524.PubMedCrossRef 18. Kanamaru

S, Kurazono H, Ishitoya S, Terai A, Habuchi T, Nakano M, Ogawa O, Yamamoto S: Distribution and genetic association of putative uropathogenic virulence factors EPZ-6438 in vitro iroN, iha, kpsMT, ompT and usp in Escherichia coli isolated from urinary tract infections in Japan. J Urol 2003,170(6 Pt 1):2490–2493.PubMedCrossRef 19. Fischbach MA, Lin H, Zhou L, Yu Y, Abergel RJ, Liu DR, Raymond KN, Wanner BL, Strong RK, Walsh CT, Aderem A, Smith KD: The pathogen-associated iroA gene cluster mediates bacterial evasion of lipocalin 2. Proc Natl Acad Sci U S A 2006,103(44):16502–16507.PubMedCrossRef 20. Cobimetinib Johnson TJ, Siek KE, Johnson SJ, Nolan LK: DNA sequence

of a ColV plasmid and prevalence of selected plasmid-encoded virulence genes among avian Escherichia coli strains. J Bacteriol 2006,188(2):745–758.PubMedCrossRef 21. Lin H, Fischbach MA, Liu DR, Walsh CT: In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. J Am Chem Soc 2005,127(31):11075–11084.PubMedCrossRef 22. Zhu M, Valdebenito M, Winkelmann G, Hantke K: Functions of the siderophore esterases IroD and IroE in iron-salmochelin utilization. Microbiology 2005,151(Pt 7):2363–2372.PubMedCrossRef 23. Bindereif A, Neilands JB: Aerobactin genes in clinical isolates of Escherichia coli. J Bacteriol 1985,161(2):727–735.PubMed 24. Carbonetti NH, Williams PH: A cluster of five genes specifying the aerobactin iron uptake system of plasmid ColV-K30. Infect Immun 1984,46(1):7–12.PubMed 25. Gross R, Engelbrecht F, Braun V: Genetic and biochemical characterization of the aerobactin synthesis operon on pColV. Mol Gen Genet 1984,196(1):74–80.PubMedCrossRef 26. Garenaux A, Caza M, Dozois CM: The Ins and Outs of siderophore mediated iron uptake by extra-intestinal pathogenic Escherichia coli. Vet Microbiol 2011,153(1–2):89–98.PubMedCrossRef 27. Kaper JB, Nataro JP, Mobley HL: Pathogenic Escherichia coli. Nat Rev Microbiol 2004,2(2):123–140.PubMedCrossRef 28.

My confidence returned. Now, perhaps, we are on some more equal footing than earlier. I wish him for his birthday continued pleasure ITF2357 concentration and success in what he is doing and a little free time to look back at a fulfilled life as one of the pioneers of photosynthesis. Jane F. Hill Botanist and a Historian of Science Bethesda, MD In addition to his own major contributions to photosynthesis research and the history of that research, Govindjee has been a mentor and inspiration to many students and

researchers in both areas. He has guided me, and many others, with unfailing encouragement and support. He encouraged me to pursue my interest in the early pioneers of photosynthesis research, culminating in a chapter that I wrote on the subject for volume 34 (Photosynthesis: Plastid Biology, Energy Conversion and Carbon Assimilation) of his series Advances in Photosynthesis and Respiration (edited by Julian Eaton-Rye (author of this article), Baishnab Tripathy (a former student of his former student late Prasanna Mohanty) and Thomas Sharkey (who is co-editor, with Govindjee,

of the series)). Subsequently, he provided me further encouragement and guidance when I told him of my interest in translating from French into English an 1804 book by the Swiss plant physiologist Théodore de Saussure, who was the last of the early photosynthesis pioneers. That translation, for which he graciously contributed a foreword, included a lengthy introduction selleck products and other background material prepared by me. It was VX-689 manufacturer published

in 2013 by Springer as nearly “Chemical Research on Plant Growth: A translation of Théodore de Saussure’s Recherches chimiques sur la Végétation”. André Jagendorf Emeritus Professor, Department of Plant Biology Cornell University, Ithaca, NY Govindjee has made important contributions to the analysis of photosynthetic mechanisms, over the whole of his professional life. His work has been especially useful in defining the role of carbon dioxide in Photosystem II, and in the insightful use of fluorescence transients. However, I think an even larger contribution has been in prolific and highly extensive writing and editing. Partly this was through his efficient editing of the journal, Photosynthesis Research; it was partly done by organizing many symposia, and monographs. His exposition of photosynthetic mechanisms, his bringing in the writings by an enormous number of scientists, has helped all of us understand much more about the integrated processes involved in photosynthesis. He has, to a large extent, become the glue bringing together many workers and many aspects of this important section of plant biology. I think of Govindjee as being the heart of the community. We are all grateful for his energy and enthusiasm in unifying our field.

Representative sections of each specimen were stained with haematoxylin-eosin to confirm the diagnosis of endometriosis. selleck products For immunohistochemistry 5-7 μm specimen sections embedded in paraffin, were cut, mounted on glass and dried overnight at 37°C. All sections were then deparaffinized in xylene, rehydrated through a graded alcohol series and washed in phosphate-buffered saline (PBS). PBS was used for all subsequent washes and for antiserum dilution. Tissue sections were quenched sequentially in 3% hydrogen peroxide in aqueous solution and blocked with PBS-6% non-fat

dry milk (Biorad, Hercules, CA, U.S.A.) for 1 h at room temperature. Slides were then incubated at 4°C overnight at 1:100 dilution with a rabbit polyclonal antibody for AMH (Abcam, Cambridge, UK). After three washes in PBS to remove the excess of antiserum, the slides were

incubated with diluted goat anti-rabbit biotinylated antibody (Vector Laboratories, Burlingame, CA, U.S.A.) at 1:200 dilution in PBS-3% non-fat dry milk (Biorad) for 1 h. All the slides were then processed by the ABC method (Vector Laboratories) for 30 min at room temperature. Diaminobenzidine (Vector Laboratories) was used as the final chromogen and hematoxylin was used as AZD1480 solubility dmso the nuclear counterstain. Negative controls for each tissue section were prepared by leaving out the primary antiserum. All samples were processed under the same conditions. Experiments were performed in compliance with the Helsinki Declaration and the protocols were approved by the ethics committee of the Fondazione Italiana Endometriosi. Cell lines and primary cells Human endometriosis stromal and epithelial cells were described elsewhere [13]. Cells

were grown following standard procedures and were propagated in DMEM/F12 (1:1) with 10% Fetal Bovine Serum (FBS) (Gibco, Life selleck compound Technologies Italia, Monza, Italy), 2 mM L-Glutamine (Euroclone S.p.a, Piero, Italy) and antibiotics (100 U/mL penicillin, 100 μg/mL streptomycin and 250 ng/mL amphotericin-B). In vitro treatment with AMH Cultured human endometrial stromal and epithelial cells were treated with Recombinant Human Mullerian-Inhibiting Substance (rhMIS)/anti-Mullerian hormone (AMH) – E-Coli derived (R&D Systems) enough and Purified recombinant protein of Homo sapiens AMH (OriGene Technologies, Rockville, MD, USA) at three different final concentrations (10-100-1000 ng) for three different time (24-48-72 hrs). Plasmin-cleaved AMH was used instead of the full-length molecule for incubation times indicated. AMH was digested by Plasmin from human plasma (Sigma-Aldrich, Italia) 1 h at 37°C in a ratio of 25 to 1, as described [14]. The effect of AMH on the activity of cytochrome P450 aromatase (CYP19) was measured through the P450-Glo assays (Promega Italia, Milano, Italy) [15].

a, b Four-spored and 8-spored asci. c Released ascospores. Scale bars: a–c = 10 μm ≡ Sphaeria calvescens Fr.

Scleromyc. Sueciae 401. Ascomata not examined. Peridium not examined. Hamathecium of dense, long, narrow cellular pseudoparaphyses, 2–3 μm broad, septate, branching and anastomosing. Asci 90–110 × 10–12 μm, 8-spored, rarely 4-spored, bitunicate, fissitunicate, cylindro-clavate, with a thick, furcate pedicel which is up to 30 μm long (Fig. 22a and b). Ascospores 13–18 × 5.5–7 μm, obliquely uniseriate and partially overlapping, broadly fusoid to oblong with broadly rounded ends, pale brown, 2-3-septate, constricted at the septa, containing four refractive globules (Fig. 22c). Note: The specimen is ACY-1215 price only a slide, and no peridium or ascomata information could be obtained. Anamorph: coelomycetous, conidia yellowish, 1-septate, 9–13 × 4–5(−8) μm (Webster and Lucas 1959); Microdiplodia henningsii Staritz=Chaetodiplodia caudina Karst. (Sutton 1980) (referred to Barr 1990b (p50)). Material examined: SWEDEN, sub-collection: Curtis Herbarium, verified by R.A. Shoemaker, leg. E.M. Fries 401 (FH-81113, isotype, microscope slide). Notes Morphology Chaetoplea was introduced based on C. calvescens, which has been regarded as similar to Pleospora or Leptosphaeria (Eriksson

and Hawksworth 1987; Wehmeyer 1961; von Arx and Müller 1975). Based on the differences in ascomata, peridium structure, pseudoparaphyses as well as its anamorphic stage, Chaetoplea was maintained as a separate genus (Barr 1990b; Yuan and Barr 1994). Chaetoplea sensu lato was accepted by Barr (1990b), which included Smoothened Agonist purchase some species SPTLC1 of Teichospora as well as the subgenus Pleospora subg. Cylindrosporeae. The following is from the label of specimen. “Sphaeria calvescens, Scler. Suecicae

(Ed. 2) 401. No specimen of Scler. Suecicae 401 is now at Uppsala according to R. Santesson 1966. This Curtis Herbarium specimen in the Farlow Herbarium is isotype. Wehmeyer (1961) in his Pleospora monograph did not study any portion of the Scler. Suecicae exsiccatus 401, nor did Webster & Lucas in the taxonomic and life-history study (Trans. Brit. Myc. Soc. 42, 332–342. 1959) of this species. The specimen has most of the features described by Webster & Lucas including the presence of the conidial state Microdiplodia henningsii Staritz. I did not see vertical septa in the ascospores. Webster & Lucas note that vertical septa may be occasionally be lacking. The fungus is otherwise as they describe it although some perithecia collapse and appear cupulate.”—by R.A. Shoemaker. Phylogenetic study None. Concluding remarks The substrate of Chaetoplea sensu Barr (1990b) can be herbaceous stalks, decorticated wood or periderm, or old cotton cloth and string, which may indicate its heterogeneous nature. The ascospores seem very much like Tariquidar cell line Phaeosphaeria which may be an earlier name; more details concerning the ascomatal, peridial and hamathecial structures are needed to make any conclusion.

PLoS Negl Trop Dis 2009,3(12):e558.PubMedCrossRef 35. Kosuwin R, Putaporntip C, Pattanawong U, Jongwutiwes S: Clonal diversity in Giardia duodenalis isolates from Thailand: evidences for intragenic recombination and purifying selection at the beta giardin locus. Gene 2010, 449:(1–2):1–8.PubMedCrossRef 36. Cock JM, Schmidt RR: Torin 2 mw A glutamate dehydrogenase gene sequence. Nucleic Acids Res 1989,17(24):10500.PubMedCrossRef 37. Geurden T, Levecke B, Caccio SM, Visser A, De Groote G, Casaert S, Vercruysse J, Claerebout E: Multilocus genotyping of Cryptosporidium and Giardia in non-outbreak related cases of diarrhoea in human patients in Belgium. Parasitology 2009,136(10):1161–1168.PubMedCrossRef

38. Ramesh MA, Malik SB, Logsdon JM Jr: A phylogenomic inventory of meiotic genes; evidence for sex in Giardia and an early eukaryotic origin of meiosis. Curr Biol 2005,15(2):185–191.PubMed 39. Lasek-Nesselquist E, Welch DM, Thompson RC, Steuart RF, Sogin ML: Genetic

exchange within and between assemblages of Giardia duodenalis . J Eukaryot Microbiol 2009,56(6):504–518.PubMedCrossRef 40. Posada D: Evaluation of methods for detecting recombination from DNA sequences: empirical data. Mol Biol Etomoxir order Evol 2002,19(5):708–717.PubMed 41. Lemey P, Posada D: Introduction to recombination detection. In The Phylogenetic Handbook: A Practical Approach to Phylogenetic Analysis and Hypothesis Testing. 2nd edition. Edited by: Lemey P, Salemi M, and Vandamme AM. New York: Cambridge University

Press; 2009:493–518. 42. Posada D: jModelTest: phylogenetic model averaging. Mol Biol Evol 2008,25(7):1253–1256.PubMedCrossRef Authors’ contributions SS participated in the study design, carried out most of experiments, analyzed and interpreted the data, and co-wrote the manuscript. SL, MM, Amylase and AT participated in the study design, EPZ015666 supervised the experiments, and co-wrote the manuscript. WS participated in specimen collection. PB participated in DNA extraction. PT conceived the project, supervised the experiments and co-wrote the manuscript. All authors read and approved the final manuscript.”
“Background Type III secretion systems (T3SS) of bacterial pathogens translocate effector proteins into infected cells resulting in a variety of modulations and disruptive actions to host cellular processes. Examples include preventing phagocytosis [1–4], altering Rho signalling [5, 6], subverting intracellular membrane trafficking [7–10] and manipulating innate immune responses [11–16]. T3SS are composed of at least 10 conserved proteins [17] some of which are present in multiple copies. Specific protein components form an export apparatus within the inner membrane. A needle complex is formed using the general secretory pathway (sec system) for some of the ‘ring’ forming components located in the inner and outer bacterial membrane.

Phosphomannomutase is responsible for conversion of mannose-6-phosphate to mannose-1-phosphate. Furthermore, manB is flanked by galU, a glucose pyrophosphorylase, and csrA, a putative carbon storage regulator (Table 3 and additional file 2, Figure S1). Genome annotation also identified the presence of a ~19 kb region that contains a cluster of genes predicted to encode for glycosyltransferases,

transport proteins, and other proteins involved in polysaccharide biosynthesis (Table 3 and additional click here file 2, Figure S1). The G+C content (36%) of this locus was similar to that of H. somni genomes (37%) [2, 25]. Table 3 Putative EPS genes in H.somni 2336 and 129Pt with proposed roles in polysaccharide synthesis Gene ORF (HSM-H. somni 2336 and HS- H. somni 129Pt) Protein annotation No. of amino acids, predicted mass (kDa) % Similarity to another protein galU HSM_1063 HS_1117 UTP-glucose-1-phosphate uridylyltransferase 295, 32.2 70, to glucose-1-phosphate uridylyltransferase, galU (E. coli) manB

HSM_1062 HS_1118 Phosphomannomutase 454, 50.3 81, to phosphomannomutase, cpsG (E. coli) csrA HSM_1061 HS_1119 Carbon storage regulator 60, 6.75 89, to pleiotropic regulatory protein for carbon source metabolism, csrA (E. coli) pldB HSM_1242 HS_0775 Lysophospholipase selleck kinase inhibitor 318, 37.4 49, to lysophospholipase L2, pldB (E. coli) ybhA HSM_1241 HS_0774 Haloacid dehalogenase-like hydrolase 273, 30.8 60, to phosphatase//phospho transferase, ybhA (E. coli) araD HSM_1240 HS_0773 L-ribulose-5-phosphate 4-epimerase 231, 25.8 82, to L-ribulose-5-phosphate 4-epimerase, Adenosine yiaS (E. coli) sgbU HSM_1239 HS_0772 Putative L-xylulose-5-phosphate 3-epimerase 290, 33.2 84, to Semaxanib L-xylulose 5-phosphate 3-epimerase, yiaQ (E. coli) rmpA HSM_1238 HS_0771 3-keto-L-gulonate-6-phosphate decarboxylase 215, 23.6 64, to 3-keto-L-gulonate 6-phosphate decarboxylase, yiaQ (E. coli) xylB HSM_1237 HS_0770 L-xylulose kinase 484, 53.7 75, to L-xylulose kinase, lyxK (E. coli) rbs1C HSM_1236

HS_0769 Ribose ABC transporter, permease 342, 32.9 59, to D-ribose transporter subunit, rbsc (E. coli) rbs1A HSM_1235 HS_0768 Ribose ABC transporter, ATPase component 496, 56.1 60, to D-ribose transporter subunit, ATP-binding component, rbsA (E. coli K12) rbs1B HSM_1234 HS_0767 ABC-type sugar transport system, periplasmic component 312, 31.0 56, to D-ribose transporter subunit, periplasmic component (E. coli ) glsS HSM_1233 HS_0766 Gluconolaconase 295, 32.6 46, to gluconolactonase, gnl (Zymomonas mobilis) rbs2B HSM_1232 HS_0765 ABC-type sugar-binding periplasmic protein 369, 37.2 81, to hypothetical protein (Yersinia intermedia ATCC 29909) rbs2C HSM_1231 HS_0764 Ribose ABC transporter, permease 349, 36.9 90, to inner-membrane translocator (Yersinia intermedia ATCC 29909) rbs2A HSM_1230 HS_0763 Ribose ABC transporter, ATPase component 505, 55.