The anomeric configuration of L-rhamnose in uridine 5'-diphosphate rhamnose and thymidine 5'-diphosphate rhamnose.
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Animals↗
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Isomeric, anti-rhamnose antibodies having specificity for rhamnose-containing, streptococcal heteroglycans.
L-Rhamnose (6-deoxy-L-mannose) is a constituent carbohydrate unit of microbial, immunogenic heteroglycans and lipopolysaccharides, and often functions as the immunodeterminant group of such immunogens. Two types of anti-rhamnose antibody have now been isolated by affinity chromatography of immune sera obtained from rabbits immunized with vaccines of Streptococcus mutans, strain KI-R, and Streptococcus pneumoniae, type 32. The antibodies of one type were directed at a glycan of L-rhamnose, D-glucose, and D-galactose in the cell wall of S. mutans, and those of the other type, against a capsular glycan of L-rhamnose and D-glucose from S. pneumoniae. The two types of anti-rhamnose antibody were immunologically distinct, and showed no reciprocal cross-reactivity. Additional properties of the two types of antibody were determined; thus, both types of antibody were of the IgG class of immunoglobulins, both possessed molecular weights of 1.45 X 10(5), and both consisted of multiple or isomeric forms.
Antibody Specificity↗
Preparation of 2-, 3-, and 4-deoxy derivatives of L-rhamnose, and derivatives of 2-azido-2-deoxy-L-rhamnose and 2,6-dideoxy-2-fluoro-L-glucose, for use in glycosylation reactions.
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Antibiotics, Antineoplastic↗
Synthesis of 3- and 4-O-beta-D-galactopyranosyl-L-rhamnose, and of 3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-rhamnose, and their use in precipitin inhibition studies with type VII antipneumococcal serum.
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Acetamides↗
1H-N.m.r. study of L-rhamnose, methyl alpha-L-rhamnopyranoside, and 4-o-beta-D-galactopranosyl-L-rhamnose in deuterium oxide.
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Galactosides↗
Metabolism of L-rhamnose in Arthrobacter pyridinolis.
In Arthrobacter pyridinolis, a respiration-coupled transport system for L-rhamnose caused accumulation of free L-rhamnose, while a phosphoenolpyruvate: L-rhamnose phosphotransferase system caused accumulation of L-rhamnose I-phosphate (Levinson & Krulwich, 1974). The pathways for subsequent metabolism of L-rhamnose and L-rhamose I-phosphate have now been investigated. Arthrobacter pyridinolis contains an inducible L-rhamnose isomerase and L-rhamnulokinase, as well as a constitutive L-rhamnulose I-phosphate aldolase. Results with mutants which are unable to metabolize L-rhamnose suggest the presence of an L-rhamnose I-phosphate phosphatase, which forms free L-rhamnose by hydrolysis of L-rhamnose I-phosphate produced by the phosphotransferase system. Mutants which lack this enzyme exhibited severe inhibition of growth in the presence of L-rhamnose plus any of a variety of carbon sources. There is some evidence that this inhibition was due to accumulation of L-rhamnose I-phosphate at toxic concentrations within the bacteria. The metabolism of L-rhamnose transported by the phosphotransferase system therefore appears to occur by hydrolysis of L-rhamnose I-phosphate to free L-rhamnose by a phosphatase. Metabolism of the L-rhamnose thus produced, and of that accumulated by the respiration-coupled transport system, the proceeds by the sequence of reactions: L-rhamnose leads to L-rhamnulose leads to L=rhamnulose I-phosphate leads to dihydroxyacetone phosphate plus L-lactaldehyde.
Aldehyde-Lyases↗
Proton-linked L-rhamnose transport, and its comparison with L-fucose transport in Enterobacteriaceae.
1. An alkaline pH change occurred when L-rhamnose, L-mannose or L-lyxose was added to L-rhamnose-grown energy-depleted suspensions of strains of Escherichia coli. This is diagnostic of sugar-H+ symport activity. 2. L-Rhamnose, L-mannose and L-lyxose were inducers of the sugar-H+ symport and of L-[14C]rhamnose transport activity. L-Rhamnose also induced the biochemically and genetically distinct L-fucose-H+ symport activity in strains competent for L-rhamnose metabolism. 3. Steady-state kinetic measurements showed that L-mannose and L-lyxose were competitive inhibitors (alternative substrates) for the L-rhamnose transport system, and that L-galactose and D-arabinose were competitive inhibitors (alternative substrates) for the L-fucose transport system. Additional measurements with other sugars of related structure defined the different substrate specificities of the two transport systems. 4. The relative rates of H+ symport and of sugar metabolism, and the relative values of their kinetic parameters, suggested that the physiological role of the transport activity was primarily for utilization of L-rhamnose, not for L-mannose or L-lyxose. 5. L-Rhamnose transport into subcellular vesicles of E. coli was dependent on respiration, was optimal at pH 7, and was inhibited by protonophores and ionophores. It was insensitive to N-ethylmaleimide or cytochalasin B. 6. L-Rhamnose, L-mannose and L-lyxose each elicited an alkaline pH change when added to energy-depleted suspensions of L-rhamnose-grown Salmonella typhimurium LT2, Klebsiella pneumoniae, Klebsiella aerogenes, Erwinia carotovora carotovora and Erwinia carotovora atroseptica. The relative rates of subsequent acidification varied, depending on both the organism and the sugar. L-Fucose promoted an alkaline pH change in all the L-rhamnose-induced organisms except the Erwinia species. No L-rhamnose-H+ symport occurred in any organism grown on L-fucose. 7. All these results showed that L-rhamnose transport into the micro-organisms occurred by a system different from that for L-fucose transport. Both systems are energized by the trans-membrane electrochemical gradient of protons. 8. Neither steady-state kinetic measurements nor binding-protein assays revealed the existence of a second L-rhamnose transport system in E. coli.
Binding, Competitive↗
L-lyxose metabolism employs the L-rhamnose pathway in mutant cells of Escherichia coli adapted to grow on L-lyxose.
Escherichia coli cannot grow on L-lyxose, a pentose analog of the 6-deoxyhexose L-rhamnose, which supports the growth of this and other enteric bacteria. L-Rhamnose is metabolized in E. coli by a system that consists of a rhamnose permease, rhamnose isomerase, rhamnulose kinase, and rhamnulose-1-phosphate aldolase, which yields the degradation products dihydroxyacetone phosphate and L-lactaldehyde. This aldehyde is oxidized to L-lactate by lactaldehyde dehydrogenase. All enzymes of the rhamnose system were found to be inducible not only by L-rhamnose but also by L-lyxose. L-Lyxose competed with L-rhamnose for the rhamnose transport system, and purified rhamnose isomerase catalyzed the conversion of L-lyxose into L-xylulose. However, rhamnulose kinase did not phosphorylate L-xylulose sufficiently to support the growth of wild-type E. coli on L-lyxose. Mutants able to grow on L-lyxose were analyzed and found to have a mutated rhamnulose kinase which phosphorylated L-xylulose as efficiently as the wild-type enzyme phosphorylated L-rhamnulose. Thus, the mutated kinase, mapped in the rha locus, enabled the growth of the mutant cells on L-lyxose. The glycolaldehyde generated in the cleavage of L-xylulose 1-phosphate by the rhamnulose-1-phosphate aldolase was oxidized by lactaldehyde dehydrogenase to glycolate, a compound normally utilized by E. coli.
Acetaldehyde↗
Use of L-rhamnose to study irreversible adsorption of bacteriophage PL-1 to a strain of Lactobacillus casei.
L-rhamnose has been found to be useful to investigate the process of irreversible adsorption of PL-I phage to its host bacterium, Lactobacillus casei ATCC27092. L-rhamnose inhibited phage adsorption to cells without inactivating free phages. Adsorption inhibition was correlated with the concentrations of L-rhamnose. The inhibitory effect of L-rhamnose on phage adsorption was of a competitive nature against host cells. Among other saccharides tested, L-fucose, L-mannose and D-ribose showed a slight degree of adsorption-inhibiting activity. In early stages of phage adsorption in a tris-maleate buffer, where the binding of phages to cells was still reversible, addition of L-rhamnose resulted in the partial desorption of phages from the cells to which they had adsorbed. However, the number of infective phages desorbed by L-rhamnose treatment gradually fell off as incubation continued, showing that the phages became firmly bound to the cells. Therefore, it is possible to determine the number of phages irreversibly adsorbed to cells by using this desorption technique with L-rhamnose. The process of irreversible phage adsorption, that is, the formation of phage-cell complexes from which no more infective phages could be desorbed, was dependent on temperature and strongly inhibited at 0 degrees C.
Adsorption↗
Differentiation of Streptococcus sanguis and S. mitior by whole-cell rhamnose content and possession of arginine dihydrolase.
Whole-cell rhamnose concentrations were measured in 48 strains of streptococci resembling Streptococcus sanguis and S. mitior. Physiological characteristics were tested by the API-20/Strep system, and it was found that "typical" S. sanguis (arginine positive, aesculin positive) contained significant amounts of rhamnose, while "typical" S. mitior (arginine negative, aesculin negative) contained very low or undetectable amounts of rhamnose. Both groups contained dextran-positive and dextran-negative strains. Organisms that were more difficult to speciate (those giving positive results in the arginine or the aesculin test, but not in both) could also be divided into a rhamnose-positive and a rhamnose-negative group; with one exception, all of the rhamnose-positive strains gave a positive result with arginine in the API-20/Strep test. There were several discrepancies between the results of conventional tests for arginine and aesculin hydrolysis and those of the corresponding API test. The results of conventional tests for arginine hydrolysis did not correlate closely with rhamnose content, and conventional tests for aesculin hydrolysis were less sensitive than API tests. With the API-20/Strep system, S. sanguis can almost always be distinguished from S. mitior by its ability to hydrolyse arginine.
Arginine↗
L-Rhamnose utilisation in Salmonella typhimurium.
L-Rhamnose is degraded by strains of Salmonella typhimurium by isomerisation to L- rhamnulose , phosphorylation to L- rhamnulose -1-phosphate and cleavage to lactaldehyde and dihydroxyacetone phosphate. The enzymes involved are, respectively, rhamnose isomerase ( RhaI ), rhamnulokinase ( RhuK ) and an aldolase (Ald). Strains able to grow rapidly on L-rhamnose contained a high-affinity uptake system for 3H-L-rhamnose that was induced by L-rhamnose and repressed by D-glucose. The synthesis of RhaI and RhuK was also induced by L-rhamnose but was not repressed by D-glucose. The synthesis of Ald was constitutive. Data are presented on some strains which grow very slowly on L-rhamnose and on others which do not utilise it.
Mutation↗
The bacteriophage kh receptor of Lactococcus lactis subsp. cremoris KH is the rhamnose of the extracellular wall polysaccharide.
A receptor for bacteriophages of lactic acid bacteria, including Lactococcus lactis subsp. cremoris KH, was found on the cell wall and not on the cell membrane, as determined by a phage-binding assay of sodium dodecyl sulfate- and mutanolysin-treated cell walls. The cell wall carbohydrates of L. lactis subsp. cremoris KH were analyzed by gas chromatography and mass spectrometry and found to contain rhamnose, galactose, glucose and N-acetylglucosamine. Similar analysis of mutants that were reduced in the ability to bind phages kh, 643, c2, ml3, and 1 indicated that galactose was essential for binding all phages. In addition, rhamnose was required for binding phages kh and ml3. Inhibition studies of phage binding by using two different lectins with a specificity for galactose indicated that phage kh may not bind directly to galactose. Rather, galactose may be an essential structural component located in the vicinity of the receptor. Incubation of any of the five phages with rhamnose or of phage kh with purified cell walls inactivated the phages. Inactivation required divalent cations and was irreversible. Inactivation of phages was stereospecific for rhamnose, as neither L-(+)- nor D-(-)-fucose (the stereoisomers of rhamnose) inhibited the phage. Furthermore, phage infection of a culture was completely inhibited by the addition of rhamnose to the medium. Therefore, the receptor for phage kh appears to be a rhamnose component of the extracellular wall polysaccharide.
Bacteriophages↗
Lactulose, 51Cr-labelled ethylenediaminetetra-acetate, L-rhamnose and polyethyleneglycol 400 [corrected] as probe markers for assessment in vivo of human intestinal permeability.
The urinary excretion of lactulose, 51Cr-labelled ethylenediaminetetra-acetate (51Cr-EDTA), L-rhamnose and polyethyleneglycol 400 (PEG-400) has been measured after intravenous and oral administration in healthy volunteers. Intestinal permeation of the probes was compared after their ingestion in iso-osmolar, hyperosmolar and cetrimide-containing test solutions. Urinary recovery of lactulose and 51Cr-EDTA after intravenous administration reached 75% by 5 h, and exceeded 90% at 24 h, and these values were 62 and 72%, respectively, for L-rhamnose. Recovery of PEG-400, however, varied with the relative molecular mass (Mr) of each polymer from 25.9 to 68.5% in 24 h. Intestinal permeation of ingested lactulose and 51Cr-EDTA was low, but that of L-rhamnose was 45-fold, and that of PEG-400 100-fold, greater. Permeation of lactulose and 51Cr-EDTA was markedly increased by cetrimide and hyperosmolar stress, whereas that of L-rhamnose showed little change. PEG-400 permeation was not affected by cetrimide, but was slightly increased by hyperosmolar stress. The 5 h permeation of lactulose, but not of L-rhamnose or PEG-400, correlated with that of 51Cr-EDTA (r = 0.98, P less than 0.001). These findings are compatible with three distinct pathways of unmediated mucosal permeation, L-rhamnose (radius less than 0.4 nm) passing mainly through small aqueous 'pores' of high incidence, lactulose and 51Cr-EDTA (radius greater than 0.5 nm) through larger aqueous 'channels' of low incidence susceptible to cetrimide and hyperosmolar stress, and PEG-400, which has appreciable lipid solubility, by partition through cell membrane lipid as well as the aqueous 'pores'.
Cell Membrane Permeability↗
The absence of rhamnose in human urine following the ingestion of gum karaya (Sterculia).
Urinary rhamnose estimations following ingestion of gum karaya were requested by the Scientific Committee for Food (EEC) in July 1983. Five male volunteers have therefore made 24-h urine collections prior to, and following, the ingestion of 10 g gum karaya for 15 days, an intake ten-fold greater than that approved in terms of the present temporary ADI (0-12 X 5 mg/kg b.w.). Paper chromatographic separations, with two solvent systems, were made on the fresh urine specimens and also after ten-fold enrichments of all urinary constituents. Standard aqueous solutions of rhamnose, and urine to which rhamnose had been added, showed the detection limit to be 0.2 microgram rhamnose. Independent examinations in two laboratories failed to detect rhamnose at this level in any of the urine specimens, Had 1% of the rhamnose present in 10 g gum karaya appeared in the 24-h urine specimens, it would have been detected. This confirms previous evidence that dietary gum karaya is neither digested nor degraded by enteric bacteria and is not absorbed to any significant extent in Man.
Adult↗
Lactulose-rhamnose intestinal permeability in children with cystic fibrosis.
The lactulose-rhamnose intestinal permeability test was performed in 10 cystic fibrosis (CF) children. Urine was collected for 5 h after oral intake of the test solution. A single thin-layer chromatography followed by densitometry was used for the measurement of lactulose and rhamnose concentrations in the urine specimens. The excretion of each molecule was expressed as the percentage of the orally administered dose excreted and the lactulose-rhamnose ratio was the ratio of the percentage quantities of each probe molecule excreted. The mean lactulose-rhamnose excretion ratio in CF patients and controls was 0.16 and 0.038, respectively (p less than 0.001). The mean 5-h lactulose excretion was 2% and 0.28% in CF patients and control subjects, respectively (p less than 0.001). The mean 5-h rhamnose excretion was 12.8% and 7.6% in CF patients and control subjects (p less than 0.05). We conclude that CF patients have an increased intestinal permeability to lactulose and rhamnose. Further studies are needed in order to elucidate the mechanisms involved as well as the eventual nutritional implications.
Adolescent↗
Cross-induction of the L-fucose system by L-rhamnose in Escherichia coli.
Dissimilation of L-fucose as a carbon and energy source by Escherichia coli involves a permease, an isomerase, a kinase, and an aldolase encoded by the fuc regulon at minute 60.2. Utilization of L-rhamnose involves a similar set of proteins encoded by the rha operon at minute 87.7. Both pathways lead to the formation of L-lactaldehyde and dihydroxyacetone phosphate. A common NAD-linked oxidoreductase encoded by fucO serves to reduce L-lactaldehyde to L-1,2-propanediol under anaerobic growth conditions, irrespective of whether the aldehyde is derived from fucose or rhamnose. In this study it was shown that anaerobic growth on rhamnose induces expression of not only the fucO gene but also the entire fuc regulon. Rhamnose is unable to induce the fuc genes in mutants defective in rhaA (encoding L-rhamnose isomerase), rhaB (encoding L-rhamnulose kinase), rhaD (encoding L-rhamnulose 1-phosphate aldolase), rhaR (encoding the positive regulator for the rha structural genes), or fucR (encoding the positive for the fuc regulon). Thus, cross-induction of the L-fucose enzymes by rhamnose requires formation of L-lactaldehyde; either the aldehyde itself or the L-fuculose 1-phosphate (known to be an effector) formed from it then interacts with the fucR-encoded protein to induce the fuc regulon.
Alcohol Oxidoreductases↗
Enzymatic synthesis and isolation of thymidine diphosphate-6-deoxy-D-xylo-4-hexulose and thymidine diphosphate-L-rhamnose. Production using cloned gene products and separation by HPLC.
A two-step enzymatic synthesis of dTDP-L-rhamnose is developed using enzymes from sonicated extracts of cultures of Escherichia coli K12 strains harboring plasmids containing different parts of the rfb gene cluster of Salmonella enterica LT2. The intermediate dTDP-6-deoxy-D-xylo-4-hexulose was isolated after a 1-h reaction, using only dTDP-D-glucose and dTDP-D-glucose 4,6-dehydratase, followed by protein precipitation and desalting by gel chromatography (yield 89%). In a two-step reaction using dTDP-D-glucose and dTDP-D-glucose 4,6-dehydratase in the first step, and with NADPH, dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase and NADPH:dTDP-6-deoxy-L-lyxo-4-hexulose-4-reductase in the second hour of incubation, the dTDP-D-glucose was fully converted to dTDP-L-rhamnose. The hexoses of both products were identified by mass spectroscopy. The molar yield of dTDP-L-rhamnose, after protein precipitation, anion-exchange chromatography and desalting by gel chromatography, was 62%, corresponding to more than 150 mg, starting from 250 mg of dTDP-D-glucose. When stored lyophilysed under nitrogen, these products were found to be stable for several months. Both dTDP-6-deoxy-D-xylo-4-hexulose and dTDP-L-rhamnose have light absorption maxima at 267 nm, with molar absorption coefficients close to that of dTMP. However, the absorption coefficient of dTDP-6-deoxy-D-xylo-4-hexulose at the absorption maximum of 320 nm (specific for sugars containing keto groups) was found to be approximately 20% higher than values presented earlier. Furthermore, an HPLC technique is presented for determining the net activity of dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase and NADPH:dTDP-6-deoxy-L-lyxo-4-hexulose-4-reductase, based on separation of dTDP-6-deoxy-D-xylo-4-hexulose and dTDP-L-rhamnose. The HPLC technique is also suitable for determination of all the nucleotide components involved in the synthesis.
Bacterial Proteins↗
Dual control of a common L-1,2-propanediol oxidoreductase by L-fucose and L-rhamnose in Escherichia coli.
Anaerobic growth of Escherichia coli on L-fucose or L-rhamnose as the sole source of carbon and energy depends on the regeneration of NAD from NADH by disposing the intermediate L-lactaldehyde as L-1,2-propanediol. The two parallel pathways, with their own permeases and enzymes encoded by two widely separated gene clusters, appear to share a single enzyme that catalyzes the formation of L-1,2-propanediol. Although this oxidoreductase is encoded by a gene at the fuc locus, the enzyme is inducible by both L-fucose and L-rhamnose. The inducibility by L-rhamnose is controlled by a gene at the rha locus with no other known functions, since the aerobic growth rate on L-rhamnose remains normal. L-1,2-Propanediol oxidoreductase activity is inducible only anaerobically, and the effect of the two methylpentoses operates at different levels: L-fucose exerts its influence post-transcriptionally; L-rhamnose exerts its influence transcriptionally.
Aerobiosis↗