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PubMed2005

Presence of glucosylceramide in yeast and its relation to alkali tolerance of yeast.

Glycosylceramide is a membrane lipid that has physiological functions in eukaryotic organisms. The presence of glucosylceramide has been confirmed in some yeast; however, the extent of the role of glucosylceramide in yeast is unknown. Thus, the extent of presence of glucosylceramide in yeast was surveyed using 90 strains of 24 genera. The strains were divided into two groups according to whether they had glucosylceramide (45 strains) or not (45 strains). The distribution of the ceramide glucosyltransferase gene (EC 2.4.1.80), which catalyzes glucosylation to a sphingoid lipid in glucosylceramide synthesis, and the phylogenetic classification of the strains were in agreement with those of glucosylceramide. Thus, the presence of glucosylceramide in yeast was caused by the presence of the gene involved in glucosylceramide synthesis and was closely associated with yeast evolution. Furthermore, the relationship between glucosylceramide presence and alkali tolerance of yeast was evaluated. The yeast with glucosylceramide tended to grow at higher pH, and a ceramide-glucosyltransferase-defective mutant from Kluyveromyces lactis did not grow at pH 8.5 even though the parent strain could grow under the same conditions. These results indicate that glucosylceramide in yeast might be a component that enables yeast to grow under alkali conditions.

Chromatography, Thin Layer↗

PubMed2006

Spatial organisation of four enzymes from Stevia rebaudiana that are involved in steviol glycoside synthesis.

The sweet steviol glycosides found in the leaves of Stevia rebaudiana Bert. are derived from the diterpene steviol which is produced from a branch of the gibberellic acid (GA) biosynthetic pathway. An understanding of the spatial organisation of the two pathways including subcellular compartmentation provides important insight for the metabolic engineering of steviol glycosides as well as other secondary metabolites in plants. The final step of GA biosynthesis, before the branch point for steviol production, is the formation of (-)-kaurenoic acid from (-)-kaurene, catalysed by kaurene oxidase (KO). Downstream of this, the first committed step in steviol glycoside synthesis is the hydroxylation of kaurenoic acid to form steviol which is then sequentially glucosylated by a series of UDP-glucosyltransferases (UGTs) to produce the variety of steviol glycosides. The subcellular location of KO and three of the UGTs involved in steviol glycoside biosynthesis was investigated by expression of GFP fusions and cell fractionation which revealed KO to be associated with the endoplasmic reticulum and the UGTs in the cytoplasm. It has also been shown by expressing the Stevia UGTs in Arabidopsis that the pathway can be partially reconstituted by recruitment of a native Arabidopsis glucosyltransferase.

Arabidopsis↗

PubMed1991

Plant biochemistry of xenobiotics: isolation and properties of soybean O- and N-glucosyl and O- and N-malonyltransferases for chlorinated phenols and anilines.

O-Glucosyltransferase (O-GT), O-malonyltransferase (O-MAT), N-glucosyltransferase (N-GT), and N-malonyltransferase (N-MAT) activities have been detected in cultured soybean cells, using pentachlorophenol and 3,4-dichloroaniline as xenobiotic standard substrates. The O-GT was purified approximately 1000-fold, and the N-MAT approximately 70-fold. There was an extensive copurification of O-GT and O-MAT. The following functional molecular weight values were obtained, 47 kDA (O-GT), 48 kDA (O-MAT) 43 kDa (N-GT), and 48 kDa (N-MAT). O-GT and N-MAT appeared to be monomeric polypeptides with isoelectric points of approximately 4.8 and approximately 6.1, respectively. The O-GT, N-GT, and N-MAT activities had marked substrate specificities for chlorinated aromatic xenobiotics and thus illustrate the existence of plant isoenzymes with specificity for xenobiotics.

Acyltransferases↗

PubMed1982

Enzymatic deoxyglucosylation of ceramides by microsomes of BHK-21 cells. The effect of deoxyglucose treatment and herpesvirus infection.

The microsomal fractions of cultured hamster fibroblasts (BHK-21 cells) catalyze the incorporation of glucose from UDPglucose or of deoxyglucose from UDPdeoxyglucose into a reaction mixture with liposomes consisting of ceramide and phosphatidylcholine. The microsomal fractions also catalyze the transfer of glucose from UDPglucose to endogenous acceptors. The specific activity of ceramide deoxyglucoside or ceramide glucoside formation was significantly higher when microsomal preparations obtained from deoxyglucose-treated or herpesvirus-infected BHK-21 cells were used as the glucosyltransferase source. Deoxyglucose was incorporated from UDPdeoxyglucose into hydroxy- and nonhydroxy-fatty acid-containing ceramides at approximately the same rate. Competitive inhibition of deoxyglucosylation of ceramides by UDPglucose suggests that both reactions were catalyzed by the same enzyme, viz. UDPglucose:ceramide glucosyltransferase. This inhibition of glycosphingolipid synthesis may account, in part, for the inhibitory effect of deoxyglucose on lipid-containing viruses.

Animals↗

PubMed1989

Control of dolichyl phosphoglucose formation in human liver microsomes. Kinetic and inhibition studies of nucleosides, nucleotides and analogues of UDPglucose.

A bisubstrate kinetic analysis of UDPglucose:dolichylphosphate glucosyltransferase from human liver microsomes has been carried out which indicated that the kinetics follow a sequential mechanism. Inhibition studies with nucleosides, nucleotides and analogues of the substrate UDPglucose revealed that the nucleoside moiety of UDPglucose, uridine, appears to be the smallest substrate analogue that is capable of specific interaction with the enzyme at the binding site for UDPglucose. The Ki values for uridine with respect to UDPglucose were 0.17 mM or 0.1 mM for enzyme reactions at pH 5.3 or pH 7.2, respectively. Modification of the uracil moiety especially at the 6 position or lack of the 2'-hydroxyl group in the ribose moiety lessened the inhibitory potency as compared to uridine. The phosphorylated derivatives of uridine, UMP and UTP, were similar in their inhibitory properties to uridine, whereas UDP was about 10-fold more potent as an inhibitor of glucosyltransferase as compared to uridine due to product inhibition. The inhibitory properties of sugar nucleotides as substrate analogues of UDPglucose were not only dependent on the presence of the uracil moiety but were also influenced by the nature of the sugar residue. Furthermore, enzyme activity was dependent on the presence of divalent metal ions and was maximally stimulated in the presence of Ca2+.

Glucosyltransferases↗

PubMed1986

Lipoprotein as a regulator of starch synthesizing enzyme activity.

Amylose precipitating factor, a lipoprotein, functions as a regulator of in vitro activity of glycogen/starch phosphorylase and of A/UDPglucose glucosyltransferase. The results suggest that this lipoprotein could act to stimulate the in vivo production by phosphorylase of long, linear glucans (amylose) from the short chain precursors. The lipoprotein also appears to switch A/UDPglucose glucosyltransferase from the elongation of branched glucan molecules (amylopectin and glycogen) to the elongation of linear glucans (amylose).

Amylose↗

PubMed1992

Action patterns of amylolytic enzymes as determined by the [1-14C]malto-oligosaccharide mapping method.

A valuable technique for oligosaccharide mapping, utilizing radioactive malto-oligosaccharides, multiple-ascent p.c., and radioautography, has been developed for identifying the action patterns of the glucoamylase isozymes, alpha-amylases, beta-amylase, glucosyltransferase, and glucanosyltransferase. The glucoamylase isozymes act by multi-chain mechanisms on malto-oligosaccharides and most likely on starch and glycogen. The alpha-amylases act endo-wise and randomly hydrolyze alpha-(1----4)- but not alpha-(1----6)-glucosidic bonds. These amylases may act by single-chain and/or multi-chain mechanisms, depending on the number of hydrolytic attacks per single encounter of the enzyme and the substrate. The beta-amylases hydrolyze malto-oligosaccharides by a multi-chain mechanism. A fungal glucosyltransferase from Aspergillus niger transfers glucose units by a single-chain mechanism from maltose to glucosyl acceptors to yield new gluco-oligosaccharides with alpha-(1----4) and alpha-(1----6) linkages. A novel type of transferase isolated from Bacillus subtilis acts by a multi-chain mechanism and transfers segments of 2 to 5 glucose residues from malto-oligosaccharides to acceptor co-substrates. An alpha-amylase from the same organism removes maltotriose units from the non-reducing ends of oligosaccharides by a multi-chain mechanism.

Amylases↗

PubMed1979

Enzymes of collagen biosynthesis in skin and serum in dermatological diseases. I. Enzymes of the skin.

Immunoreactive prolyl hydroxylase protein, prolyl hydroxylase activity and galactosylhydroxylysyl glucosyltransferase activity were measured in skin biopsies from 54 patients with various dermatological disorders and compared with results from 15 control samples; The mean prolyl hydroxylase activity was significantly elevated in case of keloids (P less than 0.001) and lichen ruber planus (P less than 0.02) and the mean galactosylhydroxylysyl glucosyltransferase activity in keloids (P less than 0.005), lichen ruber planus (P less than 0.02) and psoriasis (P less than 0.05), and high activities of these two enzymes were also occasionally found in other skin diseases and active systemic connective tissue diseases. These two enzyme activities correlated highly significantly (P less than 0.001) with each other in the total disease material. Immunoreactive prolyl hydroxylase protein was significantly elevated in psoriasis (P less than 0.02) lichen ruber planus (P less than 0.005), but not in keloids, where very high activities of the corresponding enzyme were found. Active prolyl hydroxylase constituted about 1.3% of total immunoreactive prolyl hydroxylase protein in normal skin, but as much as 10% in cases of keloids.

Adolescent↗

PubMed1987

Enzyme markers of collagen synthesis in carbon tetrachloride-induced fibrosis and during colchicine modification of CCl4-induced liver injury.

Serum galactosylhydroxylysyl glucosyltransferase (S-Glu-Gal-Hyl-Tase), liver galactosylhydroxylysyl glucosyltransferase (L-Glu-Gal-Hyl-Tase), liver hydroxylysyl galactosyltransferase (L-Gal-Hyl-Tase), and liver prolyl hydroxylase (L-PH) activities were measured in rats during the development of CCl4-induced cirrhosis (0.2 ml of 33% CCl4 in light mineral oil two times weekly for 10 weeks followed by 6 weeks of no treatment). Serum and liver markers of collagen synthesis increased in a time-dependent manner reaching maximum activity at 6 weeks (S-Glu-Gal-Hyl-Tase, two times; L-PH, two times). These enzyme levels returned to normal during the 4-week recovery period. In a separate 4-week experiment, colchicine (10 micrograms/rat/day) was administered with CCl4. Colchicine prevented the increase in S-Glu-Gal-Hyl-Tase, L-Glu-Gal-Hyl-Tase, and L-Gal-Hyl-Tase induced by CCl4 and resulted in a smaller increase in L-PH. These results demonstrate that S-Glu-Gal-Hyl-Tase elevation occurs following CCl4 because of increased liver collagen synthetic activity and the hepatocellular injury produced by CCl4.

Animals↗

PubMed1985

Serum and liver enzymes of collagen synthesis in hepatic murine schistosomiasis mansoni.

Serum galactosylhydroxylysyl glucosyltransferase (S-GGT), liver galactosylhydroxylysyl glucosyltransferase (L-GGT), liver hydroxylysyl galactosyltransferase (L-GGal-T) and liver prolyl hydroxylase (L-PH) activities were measured in CF1 female mice each week for 10 weeks after infection with Schistosoma mansoni (50 cercariae per mouse). None of the enzyme activities measured were significantly increased in the first six weeks following the infection. However, the activities increased thereafter reaching a maximum of seven-fold for S-GGT, five-fold for L-GGT, three-fold for L-GGal-T and ten-fold for L-PH compared with control animals. The increase in S-GGT activity was positively correlated with L-GGT (r = 0.788), L-GGal-T (r = 0.774) and L-PH (r = 0.800). The present data suggest that during the first six weeks of the development of murine hepatic schistosomiasis mansoni infection, few eggs bombard the liver. The biochemical changes during this period are mild. During weeks 7 to 10, which is the active fibrotic stage, the liver biochemical markers of collagen synthesis increase rapidly and lead to fibrotic morphological features that are the chronic irreversible hepatic changes characteristic of this infection. The data reported here indicate that the aggressive fibrotic changes in liver during weeks 7 to 10 of murine schistosomiasis infection are predicted by S-GGT activity.

Animals↗

PubMed1990

Effects of chronic ethanol administration on plasma-membrane-bound glycosyltransferase activities.

Physiological and membranous modifications induced by a 4-week ethanol administration in mouse liver plasma membrane were studied. Galactosyl- and glucosyltransferase activities were stimulated in the presence of dolichylphosphate alone or with phosphatidyl-choline. The galactosyltransferase activity was inhibited by chronic ethanol administration. These enzymes were modulated by different phospholipids. The phosphatidic acid was the most efficient activator. Ethanol provoked an inhibition of the galactosyltransferase activity whatever the phospholipid used, as well as an inhibition of the glucosyltransferase activity, chiefly in presence of phosphatidyl-inositol. The preincubation of control or treated mouse liver plasma membranes with liposomes loaded by dolichylphosphate and cholesterol greatly enhanced the enzymatic activities without removing the inhibition by ethanol treatment.

Alcoholism↗

PubMed2005

Changes in linkage pattern of glucan products induced by substitution of Lys residues in the dextransucrase.

Dextransucrase S (DSRS) is the only active glucansucrase that has been found in Leuconostoc mesenteroides NRRL B-512F strain. Native DSRS produces mainly 6-linked glucopyranosyl residue (Glcp), while Escherichia coli recombinant DSRS was observed to produce a glucan consisting of 70% 6-linked Glcp and 15% 3,6-Glcp. Lys residues were introduced at the N-terminal end of the core domain by site-directed mutagenesis. In glucans produced by the one-point mutants T350K and S455K, the amount of 6-linked Glcp was increased to about 85% of the total glucan produced, more similar in structure to native B-512F dextran. The double mutant T350K/S455K produced adhesive, water-insoluble glucan with 77% 6-linked Glcp, 8% 3,6-linked Glcp and 4% 2,6-linked Glcp. The T350K/S455K mutant exhibited a 10-fold increase in glucosyltransferase activity over those of the parental DSRS-His(6) and its T350K and S455K mutants. This is the first report demonstrating a change in the properties of a dextransucrase or a related glucosyltransferase through simple site-directed mutagenesis to create 2,6-linked Glcp.

Amino Acid Sequence↗

PubMed2004

Role of Helicobacter pylori rfaJ genes (HP0159 and HP1416) in lipopolysaccharide synthesis.

The genome of Helicobacter pylori 26695 has been sequenced and the lipopolysaccharide (LPS) O sidechain of this strain has been shown to express both Lewis x and Lewis y units. To determine the role of HP0159 and HP1416, genes recognized as rfaJ homologs and implicated in LPS synthesis, isogenic mutants of H. pylori 26695 were generated. The LPS of mutant 26695::HP0159Kan did not express either Lewis epitope as detected by immunoblotting, whereas the control strain and 26695::HP1416Kan produced both epitopes. Structural analysis of the LPS of the mutants showed that HP0159 encodes an alpha(1,2/3)-glucosyltransferase whereas HP1416 encodes an alpha(1,2/4)-glucosyltransferase.

Genes, Bacterial↗

PubMed2004

Inhibitory effect of some herbal extracts on adherence of Streptococcus mutans.

The objective of this study was to investigate the inhibitory effect of the crude extracts from some herbs on adherence of Streptococcus mutans (S. mutans) ATCC 25175 and TPF-1 in vitro. Six herbs, Andrographis paniculata; Cassia alata; Chinese black tea (Camellia sinensis); guava (Psidium guajava); Harrisonia perforata and Streblus asper, were extracted with 50 or 95% ethanol and dried. Herbal extracted solution at 0.5% concentration (w/v) was initially tested for bacterial adherence on glass surfaces. In order to identify type and effective concentration of the extracts, the extracts that showed the inhibition on glass surfaces were then tested on saliva-coated hydroxyapatite by the use of radiolabeled bacteria. To study the mechanism of action, the effect of the extracts at such concentration on glucosyltransferase and glucan-binding lectin activities were examined. It was found that all extracts, but Streblus asper, showed significant inhibitory effect on bacterial adherence to glass surfaces. For the saliva-coated hydroxyapatite adherence assay, Andrographis paniculata, Cassia alata, Chinese black tea and Harrisonia perforata could inhibit adherence of S. mutans ATCC 25175. Chinese black tea was the strongest inhibitor followed by Andrographis paniculata, Cassia alata and Harrisonia perforata, respectively. For S. mutans TPF-1, adherence inhibition was observed from Andrographis paniculata and Cassia alata at similar levels. The lowest concentrations of the extracts that inhibited the adherence at least 50% were 0.5% of Andrographis paniculata, 0.5% of Cassia alata, 0.3% of Chinese black tea and 0.5% of Harrisonia perforata for S. mutans ATCC 25175. For S. mutans TPF-1, the effective concentrations were 0.5% of Andrographis paniculata and 0.4% of Cassia alata. All extracts at such concentrations decreased the activity of glucosyltransferase from both strains. Only Andrographis paniculata and Cassia alata eliminated or decreased the activity of glucan-binding lectin from both strains. These findings suggested that Andrographis paniculata, Cassia alata, Chinese black tea and Harrisonia perforata could inhibit adherence of S. mutans ATCC 25175, while Andrographis paniculata and Cassia alata had an effect on S. mutans TPF-1 in vitro at the concentrations employed in this study.

Bacterial Adhesion↗

PubMed2000

In situ studies of pellicle formation on hydroxyapatite discs.

The formation of acquired enamel pellicle on hydroxyapatite (HA) discs of known surface area carried in the mouth was studied; discs were carried in the mouth for 30 s, 1, 5, 10 and 20 min. Similar amounts of protein were found on the discs at each time-point, as determined by ninhydrin analyses. The amounts of amylase and lysozyme detected remained stable after 5 min of exposure of the discs to the mouth. Assay of the discs for fructosyl- and glucosyltransferase activities revealed that fructosyltransferase activity increased up to 1 min of exposure to the mouth and decreased when kept in the mouth for longer periods; glucosyltransferase activity, in contrast, increased the longer the discs were kept in the mouth. This in situ model provides insight into the activities of various enzymes during the first 20 min of pellicle formation. The effects of rinsing with sucrose and sugar alcohols on pellicle formation on the discs were also explored. The discs were placed in the mouth for 30 s, 1, 5, 10 and 20 min, preceded by rinsing with either distilled deionized water, sucrose, sorbitol, xylitol or phosphate-buffered saline. Western blot analyses of disc eluates with antiserum/antibody preparations to various salivary components revealed distinct patterns of deposition of bacterial and salivary components depending on the composition of the rinse. These studies confirm that salivary molecules and bacteria are deposited on apatitic surfaces in a selective manner and reveal that pellicle formation may be influenced by composition of diet. It is apparent that this in situ model could be used in screening potential antiplaque agents.

Adult↗

PubMed1996

Cloning and sequencing of a gene coding for a novel dextransucrase from Leuconostoc mesenteroides NRRL B-1299 synthesizing only alpha (1-6) and alpha (1-3) linkages.

The coding region for a Leuconostoc mesenteroides NRRL B-1299 dextransucrase gene (dsrA) was isolated and sequenced. Using a pair of primers designed on the basis of two highly conserved amino-acid (aa) sequences in L. mesenteroides NRRL B-512F dextransucrase and streptococcal glucosyltransferases (GTFs), a fragment of dsrA was amplified by the polymerase chain reaction (PCR). This PCR product was used as an hybridization probe to isolate a 1.8-kb fragment identified as the central region of dsrA. Cleavage by Sac I of this fragment allowed two probes to be obtained to isolate the 5' and the 3' ends of dsrA. The nucleotide sequence of the dsrA gene was determined and found to consist of an open reading frame (ORF) of 4870 base pairs (bp) coding for a 1290-aa protein with an M(r) of 145590. The aa sequence exhibited a high similarity with other GTFs. The two domains previously described in GTFs are conserved in DSRA: an N-terminal conserved domain and a C-terminal domain composed of a series of repeats. Surprisingly, the expected signal peptide was not detected. The entire gene was reconstructed and the activity of DSRA was investigated. The dextran produced appeared to be composed of 85% alpha (1-6) and 15% alpha (1-3) linkages and the oligosaccharides synthesized in the presence of maltose were mainly composed of alpha (1-6) linkages. This enzyme is a novel dextransucrase from L. mesenteroides NRRL B-1299 producing no alpha (1-2) linkages and is the first glucosyltransferase having no signal peptide described.

Amino Acid Sequence↗

PubMed1989

Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes.

An assay for UDP-Glc:glycoprotein glucosyltransferase was developed. Incubation of rat liver microsomes with UDP-[14C]Glc led to the formation of hot trichloroacetic acid insoluble material identified as protein-linked Glc1Man7-9GlcNAc2. Addition of 8 M urea-denatured thyroglobulin to the incubation mixtures stimulated up to 10-12-fold the formation of the same compounds but only in the presence of detergents. Native thyroglobulin was ineffective. Several experiments indicated that the stimulation was due to the transfer of glucose residues from UDP-Glc to high-mannose oligosaccharides in urea-denatured thyroglobulin and that this transfer reaction did not involve dolichol mono- or diphosphate derivatives as intermediates. The glycoprotein glucosylating activity was mainly located in the endoplasmic reticulum and could glucosylate glycopeptides derived from the digestion of thyroglobulin with an unspecific protease. Glucosylation of oligosaccharides in those glycopeptides occurred, however, at a rate at least 2 orders of magnitude slower than that of the same compounds in urea-denatured thyroglobulin. Tryptic digestion of urea-denatured thyroglobulin did not affect its glucosylation rate. The structure of Glc1Man9GlcNAc2 linked to urea-denatured thyroglobulin was identical with that of Glc1Man9GlcNAc2-P-P-dolichol. The assay of UDP-Glc:glycoprotein glucosyltransferase allowed detection of the activity in microsomal membranes in which endogenous acceptors appeared to be absent or almost absent, such as those derived from mung bean, Mucor rouxii, Crithidia fasciculata, and Trypanosoma cruzi cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetylglucosaminidase↗

PubMed1999

Effect of inactivation of gtf genes on adherence of Streptococcus downei.

The activity of glucosyltransferases (GTF), a group of enzymes that synthesize water-soluble and -insoluble glucans from sucrose, significantly contributes to the cariogenicity of mutans streptococci. Streptococcus downei produces four glucosyltransferases, GTFI, which produces insoluble glucan, and GTFS, GTFT, and GTFU, which synthesize soluble glucans. We have previously reported that inactivation of gtfS results in altered adherence and have now examined its interaction with other enzymes by constructing mutants which were gtfS, gtfS/gtfT, gtfS/gtfI and gtfI. The mutants were tested for their ability to accumulate on wires and on plastic microtiter trays in the presence of sucrose. The gtfS mutant displayed a reduced ability to adhere compared to the wild type but there was no further reduction of adherence in a gtfS/gtfT mutant. In contrast, the gtfS/gtfI double mutant showed a drastic reduction in adherence and when gtfI alone was inactivated, bacteria were unable to adhere to a hard surface. The results confirmed that insoluble glucan is required for strong adherence to a smooth surface but that the amount and structure of this glucan is dependent upon the availability of soluble glucans to act as primer molecules.

Bacterial Adhesion↗