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Purification to homogeneity and properties of plant glucosidase I.

Glucosidase I was purified about 3600-fold to apparent homogeneity from the microsomal fraction of mung bean seedlings. The purified enzyme removed the terminal alpha1,2-linked glucose from Glc3Man9GlcNAc2-peptide or the endoglucosaminidase H (Endo H)-released oligosaccharide. Glucosidase I activity was inhibited by kojibiose [Glc(alpha1-2)Glc], but not by other glucose disaccharides. Removal of up to four mannose residues from the N-linked oligosaccharide had little effect on its utilization as a substrate for glucosidase I. The enzyme had a subunit molecular weight of 97 kDa on SDS gels and this was shifted to 94 kDa after treatment with Endo H or Endo F, suggesting that glucosidase I is an N-glycoprotein having one oligomannose-type oligosaccharide. Amino acid sequences of this enzyme showed considerable identity to the enzyme cloned from a human hippocampus cDNA library. The enzyme was inhibited by castanospermine, deoxynojirimycin, MDL, and trehazolin, but not by australine or kifunensine. On the other hand, the other processing glucosidase, glucosidase II, is sensitive to inhibition by australine, but not by trehazolin. Thus, these two inhibitors are useful to distinguish glucosidase I from glucosidase II. The mung bean glucosidase I is quite sensitive to the histidine modifying reagent diethyl pyrocarbonate, whereas the pig liver glucosidase I is not. On the other hand, pig liver and pig brain glucosidase I preparations are sensitive to the sulfhydryl reagent NEM (N-ethylmaleimide), whereas the plant enzyme is not. These sensitivities to amino acid modifiers suggest significant differences between the plant and animal glucosidase I, in terms of catalytic site or protein conformation.

Amino Acid Sequence↗

Enzymatic properties of two beta-glucosidases from Ceriporiopsis subvermispora produced in biopulping conditions.

AIMS: Ceriporiopsis subvermispora produces endoglucanase and beta-glucosidase when cultivated on cellulose or wood, but biodegradation of cellulose during biopulping by C. subvermispora is low even after long periods. To resolve this discrepancy, we grew C. subvermispora on Pinus taeda wood chips and purified the major beta-glucosidases it produced. Kinetic parameters were determined to clear if this fungus produces enzymes capable of yielding assimilable glucose from wood. METHODS AND RESULTS: Ceriporiopsis subvermispora was grown on P. taeda wood chips under solid-state fermentation. After 30 days, the crude extract obtained from enzyme extraction with sodium acetate buffer 50 mmol l(-1), pH 5.4, was filtrated in membranes with a molecular mass exclusion limit of 100 kDa. Enzyme purification was carried out using successively Sephacryl S-300 gel filtration. The retained fraction attained 76% of beta-glucosidase activity with 3.7-fold purification. Two beta-glucosidases were detected with molecular mass of 110 and 53 kDa. We have performed a characterization of the enzymatic properties of the beta-glucosidase of 110 kDa. The optimum pH and temperature were 3.5 and 60 degrees C, respectively. The K(m) and V(max) values were respectively 3.29 mmol l(-1) and 0.113 micromol min(-1) for the hydrolysis of p-nitrophenyl-beta-glucopyranoside (pNPG) and 2.63 mmol l(-1) and 0.103 micromol min(-1), towards cellobiose. beta-Glucosidase activity was strongly increased by Mn(2+) and Fe(3+), while Cu(2+) severely inhibited it. CONCLUSIONS: Ceriporiopsis subvermispora produces small amounts of beta-glucosidase when grown on wood. The gel filtration and polyacrylamide gel electrophoresis data revealed the existence of two beta-glucosidases with 110 and 53 kDa. The 110 kDa beta-glucosidase from C. subvermispora can be efficiently purified in a single step by gel filtration chromatography. The enzyme has an acid pH optimum with similar activity on pNPG and cellobiose and is thus typical beta-glucosidase. SIGNIFICANCE AND IMPACT OF THE STUDY: Ceriporiopsis subvermispora produces beta-glucosidase with limited action during wood decay making able its use for the production of biomechanical and biochemical pulps. The results presented in this paper show the importance of studying the behaviour of beta-glucosidases during biopulping.

Basidiomycota↗

Purification and Characterization of a Cellulose-Binding (beta)-Glucosidase from Cellulose-Degrading Cultures of Phanerochaete chrysosporium.

Extracellular (beta)-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium was purified by DEAE-Sephadex chromatography, by Sephacryl S-200 chromatography, and by fast protein liquid chromatography (FPLC) using a Mono Q anion-exchange column. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic (SDS-PAGE) analysis of FPLC-purified (beta)-glucosidase indicated the presence of three enzyme forms with molecular weights of 96,000, 98,000, and 114,000. On further fractionation with a microcrystalline cellulose column, the 114,000-molecular-weight (beta)-glucosidase, which had 82% of the (beta)-glucosidase activity, was bound to cellulose. The (beta)-glucosidases with molecular weights of 96,000 and 98,000 did not bind to cellulose. The cellulose-bound (beta)-glucosidase was eluted completely from the cellulose matrix with water. Cellulose-bound (beta)-glucosidase catalyzed p-nitrophenylglucoside hydrolysis, suggesting that the catalytic site is not involved in cellulose binding. When the cellulose-binding form was incubated with papain for 20 h, no decrease in the enzyme activity was observed; however, approximately 74% of the papain-treated glucosidase did not bind to microcrystalline cellulose. SDS-PAGE analysis of the nonbinding glucosidase produced by papain indicated the presence of three bands with molecular weights in the range of 95,000 to 97,000. On the basis of these results, we propose that the low-molecular-weight (96,000 and 98,000) non-cellulose-binding (beta)-glucosidase forms are most probably formed from the higher-molecular-weight (114,000) cellulose-binding (beta)-glucosidase via extracellular proteolytic hydrolysis. Also, it appears that the extracellular (beta)-glucosidase from P. chrysosporium might be organized into two domains, a cellulose-binding domain and a catalytic domain. Kinetic characterization of the cellulose-binding form is also presented.

Journal Article↗

Long-term intravenous treatment of Pompe disease with recombinant human alpha-glucosidase from milk.

OBJECTIVE: Recent reports warn that the worldwide cell culture capacity is insufficient to fulfill the increasing demand for human protein drugs. Production in milk of transgenic animals is an attractive alternative. Kilogram quantities of product per year can be obtained at relatively low costs, even in small animals such as rabbits. We tested the long-term safety and efficacy of recombinant human -glucosidase (rhAGLU) from rabbit milk for the treatment of the lysosomal storage disorder Pompe disease. The disease occurs with an estimated frequency of 1 in 40,000 and is designated as orphan disease. The classic infantile form leads to death at a median age of 6 to 8 months and is diagnosed by absence of alpha-glucosidase activity and presence of fully deleterious mutations in the alpha-glucosidase gene. Cardiac hypertrophy is characteristically present. Loss of muscle strength prevents infants from achieving developmental milestones such as sitting, standing, and walking. Milder forms of the disease are associated with less severe mutations and partial deficiency of alpha-glucosidase. METHODS: In the beginning of 1999, 4 critically ill patients with infantile Pompe disease (2.5-8 months of age) were enrolled in a single-center open-label study and treated intravenously with rhAGLU in a dose of 15 to 40 mg/kg/week. RESULTS: Genotypes of patients were consistent with the most severe form of Pompe disease. Additional molecular analysis failed to detect processed forms of alpha-glucosidase (95, 76, and 70 kDa) in 3 of the 4 patients and revealed only a trace amount of the 95-kDa biosynthetic intermediate form in the fourth (patient 1). With the more sensitive detection method, 35S-methionine incorporation, we could detect low-level synthesis of -glucosidase in 3 of the 4 patients (patients 1, 2, and 4) with some posttranslation modification from 110 kDa to 95 kDa in 1 of them (patient 1). One patient (patient 3) remained totally deficient with both detection methods (negative for cross-reactive immunologic material [CRIM negative]). The alpha-glucosidase activity in skeletal muscle and fibroblasts of all 4 patients was below the lower limit of detection (<2% of normal). The rhAGLU was tolerated well by the patients during >3 years of treatment. Anti-rhAGLU immunoglobulin G titers initially increased during the first 20 to 48 weeks of therapy but declined thereafter. There was no consistent difference in antibody formation comparing CRIM-negative with CRIM-positive patients. Muscle alpha-glucosidase activity increased from <2% to 10% to 20% of normal in all patients during the first 12 weeks of treatment with 15 to 20 mg/kg/week. For optimizing the effect, the dose was increased to 40 mg/kg/week. This resulted, 12 weeks later, in normal alpha-glucosidase activity levels, which were maintained until the last measurement in week 72. Importantly, all 4 patients, including the patient without any endogenous alpha-glucosidase (CRIM negative), revealed mature 76- and 70-kDa forms of -glucosidase on Western blot. Conversion of the 110-kDa precursor from milk to mature 76/70-kDa alpha-glucosidase provides evidence that the enzyme is targeted to lysosomes, where this proteolytic processing occurs. At baseline, patients had severe glycogen storage in the quadriceps muscle as revealed by strong periodic acid-Schiff--positive staining and lacework patterns in hematoxylin and eosin--stained tissue sections. The muscle pathology correlated at each time point with severity of signs. Periodic acid-Schiff intensity diminished and number of vacuoles increased during the first 12 weeks of treatment. Twelve weeks after dose elevation, we observed signs of muscle regeneration in 3 of the 4 patients. Obvious improvement of muscular architecture was seen only in the patient who learned to walk. Clinical effects were significant. All patients survived beyond the age of 4 years, whereas untreated patients succumb at a median age of 6 to 8 months. The characteristic cardiac hypertrophy present at start of treatment diminished significantly. The left ventricular mass index decreased from 171 to 599 g/m2 (upper limit of normal 86.6 g/m2 for infants from 0 to 1 year) to 70 to 160 g/m2 during 84 weeks of treatment. In addition, we found a significant change of slope for the diastolic thickness of the left ventricular posterior wall against time at t = 0 for each separate patient. Remarkably, the younger patients (patients 1 and 3) showed no significant respiratory problems during the first 2 years of life. One of the younger patients recovered from a life-threatening bronchiolitis at the age of 1 year without sequelae, despite borderline oxygen saturations at inclusion. At the age of 2, however, she became ventilator dependent after surgical removal of an infected Port-A-Cath. She died at the age of 4 years and 3 months suddenly after a short period of intractable fever of >42 degrees C, unstable blood pressure, and coma. The respiratory course of patient 1 remained uneventful. The 2 older patients, who both were hypercapnic (partial pressure of carbon dioxide: 10.6 and 9.8 kPa; normal range: 4.5-6.8 kPa) at start of treatment, became ventilator dependent before the first infusion (patient 2) and after 10 weeks of therapy (patient 4). Patient 4 was gradually weaned from the ventilator after 1 year of high-dose treatment and was eventually completely ventilator-free for 5 days, but this situation could not be maintained. Currently, both patients are completely ventilator dependent. The most remarkable progress in motor function was seen in the younger patients (patients 1 and 3). They achieved motor milestones that are unmet in infantile Pompe disease. Patient 1 learned to crawl (12 months), walk (16 months), squat (18 months), and climb stairs (22 months), and patient 3 learned to sit unsupported. The Alberta Infant Motor Scale score for patients 2, 3, and 4 remained far below p5. Patient 1 followed the p5 of normal. CONCLUSION: Our study shows that a safe and effective medicine can be produced in the milk of mammals and encourages additional development of enzyme replacement therapy for the several forms of Pompe disease. Restoration of skeletal muscle function and prevention of pulmonary insufficiency require dosing in the range of 20 to 40 mg/kg/week. The effect depends on residual muscle function at the start of treatment. Early start of treatment is required.

Animals↗

A specific acid alpha-glucosidase in lamellar bodies of the human lung.

In the present investigation, we have demonstrated that three lysosomal-type hydrolases, alpha-glucosidase, alpha-mannosidase and a phosphatase, are present in lamellar bodies isolated from adult human lung. The hydrolase activities that were studied, all showed an acidic pH optimum, which is characteristic for lysosomal enzymes. The properties of acid alpha-glucosidase in the lamellar body fraction and that in the lysosome-enriched fraction were compared. Using specific antibodies against lysosomal alpha-glucosidase from human placenta, two alpha-glucosidases could be distinguished in the lamellar body fraction: one with a high affinity to the antibodies as found in the lysosome-enriched fraction and another with a much lower affinity. Both forms showed an acidic pH optimum. The same heterogeneity of alpha-glucosidase in the lamellar body fraction could be observed using immobilized concanavalin A. The lectin was able to precipitate nearly all alpha-glucosidase activity of the lysosome-enriched fraction. In contrast, 30% of the alpha-glucosidase activity in the lamellar body fraction was not precipitable. Furthermore, the lamellar body alpha-glucosidase with the low antibody affinity could not be bound to concanavalin A. The results suggest that lamellar bodies contain at least two acid alpha-glucosidases: one similar to the lung lysosomal alpha-glucosidase, and another lamellar body-specific isoenzyme with a different immunoreactivity and lectin affinity. The lamellar body-specific alpha-glucosidase should prove useful as a lamellar body-specific marker enzyme.

Antibodies↗

Heterogeneity in human acid beta-glucosidase revealed by cellulose-acetate electrophoresis.

Cellulose-acetate gel electrophoresis, a technique commonly used for the separation of human acid hydrolases, was applied to study heterogeneity in acid beta-glucosidase (EC 3.2.1.45). With this technique, three forms of beta-glucosidase were distinguishable in extracts of several tissues. The most anodic beta-glucosidase activity (band 3) represents the broad-specificity beta-glucosidase that is not deficient in Gaucher disease and is not inhibited by conduritol B-epoxide (CBE). The beta-glucosidase activity was deficient in Gaucher disease. A third beta-glucosidase activity with an intermediate mobility (band 2) was also inhibited by CBE and deficient in Gaucher disease. Band 1 and band 2 beta-glucosidase thus represent different forms of glucocerebrosidase. By adding phosphatidylserine and sphingolipid activator protein (SAP-2), monomeric glucocerebrosidase could be completely converted into a form that comigrated with band 2 beta-glucosidase of tissue extracts. The addition of phosphatidylserine only also resulted in a changed mobility of the monomeric enzyme, but the migration in this case differed from that of band 2 beta-glucosidase of tissue extracts. The electrophoretic profile of beta-glucosidase activity of tissue extracts changed upon ethanol/chloroform extraction: the two glucocerebrosidase forms were converted into a band with a mobility identical to that of band 1 beta-glucosidase. Our findings indicate that the interaction of glucocerebrosidase with phospholipid and SAP-2 has major effects on the mobility of the enzyme in the cellulose-acetate gel electrophoresis system. The findings with the cellulose-acetate gel electrophoretic system are discussed in relation to the heterogeneity in glucocerebrosidase observed with sucrose density gradient analysis, immunochemical methods and isoelectric focussing studies.

Electrophoresis↗

Effectors of three beta-glucosidases from human liver.

1. A third beta-glucosidase from human liver has been isolated using a mild (0.02-0.10%) Triton X-100 extraction of the exhaustively washed high speed (200,000 X g, 30 min) particulate fraction, QAE-Sephadex and concanavalin A-Sepharose chromatography. This new beta-glucosidase, referred to as TX beta-glucosidase, possesses a distinctive set of chemical properties such that it is similar to both, glucocerebrosidase and cytoplasmic beta-glucosidase, but it is not identical to either enzyme. 2. The TX beta-glucosidase hydrolyzes glucocerebroside as well as the beta-D-glucose, beta-D-galactose, beta-D-fucose, beta-D-xylose and alpha-L-arabinose derivatives of 4-methylumbelliferone. Like the cytoplasmic beta-glucosidase, the TX beta-glucosidase is inhibited by bile salts, and unaffected by conduritol B epoxide and heat stable activator protein. 3. All three beta-glucosidases were inhibited by N-hexylpsychosine, and all showed the same, mixed type inhibition kinetics, indicating a common hydrophobic binding site in all three enzymes. 4. The TX beta-glucosidase, which constitutes only a few percent of the total beta-glucosidase activity of human liver, is absent from liver from two cases of neurologic Gaucher disease and present in reduced amounts in a third case with CNS disease. Liver from a case of type 1 Gaucher disease contained normal amounts of the TX beta-glucosidase.

Bile Acids and Salts↗

Expression of cytosolic beta-glucosidase in guinea pig liver cells.

The cytosolic beta-glucosidase of mammalian liver has been implicated in the metabolic transformation of plant glycosides, such as vicine and amygdalin, which are associated with the development of toxic syndromes. We investigated which cell types express cytosolic beta-glucosidase in guinea pig liver, and characterized the contribution of this enzyme to the hydrolysis of aromatic glucosides in cultured cells and in tissue slices. Cytosolic beta-glucosidase was expressed in hepatocytes and not in Kupffer or endothelial cells as determined by enzyme-specific activity and Western blots of liver cell extracts. Intracellular beta-glucosidase activity was visualized using the fluorescent beta-glucosidase substrate, resorufin beta-D-glucoside, and shown to be caused by the cytosolic beta-glucosidase using the inhibitors, conduritol beta-epoxide and dinitrophenol-2-deoxy-2-fluoro-beta-D-glucopyranoside (DNP2FGlc). Staining of fresh liver slices with resorufin beta-glucoside revealed that cytosolic beta-glucosidase is expressed in all hepatocytes, with no significant portal-central gradient. These data indicate that cytosolic beta-glucosidase is a hepatocyte-specific enzyme, and support the hypothesis that cytosolic beta-glucosidase in the liver functions to hydrolyze small glucosides absorbed by the intestine. Furthermore, toxic injury to cultured hepatocytes by CCl4 resulted in release of cytosolic beta-glucosidase in parallel with the hepatocyte marker enzymes alanine transaminase and lactate dehydrogenase. This suggests that acute increases in serum levels of cytosolic beta-glucosidase in animal models of liver injury may reflect direct injury of hepatocytes.

Animals↗

Purification and characterization of two extracellular beta-glucosidases from Trichoderma reesei.

A major beta-glucosidase I and a minor beta-glucosidase II were purified from culture filtrates of the fungus Trichoderma reesei grown on wheat straw. The enzymes were purified using CM-Sepharose CL-6B cation-exchange and DEAE Bio-Gel A anion-exchange chromatography steps, followed by Sephadex G-75 gel filtration. The isolated enzymes were homogeneous in SDS-polyacrylamide gel electrophoresis and isoelectric focusing. beta-Glucosidase I (71 kDa) was isoelectric at pH 8.7 and contained 0.12% carbohydrate; beta-glucosidase II (114 kDa) was isoelectric at pH 4.8 and contained 9.0% carbohydrate. Both enzymes catalyzed the hydrolysis of cellobiose and p-nitrophenyl-beta-D-glucoside (pNPG). The Km and kcat/Km values for cellobiose were 2.10 mM, 2.45.10(4) s-1 M-1 (beta-glucosidase I) and 11.1 mM, 1.68.10(3) s-1 M-1 (beta-glucosidase II). With pNPG as substrate the Km and kcat/Km values were 182 microM, 7.93.10(5) s-1 M-1 (beta-glucosidase I) and 135 microM, 1.02.10(6) s-1 M-1 (beta-glucosidase II). The temperature optimum was 65-70 degrees C for beta-glucosidase I and 60 degrees C for beta-glucosidase II, the pH optimum was 4.6 and 4.0, respectively. Several inhibitors were tested for their action on both enzymes. beta-Glucosidase I and II were competitively inhibited by desoxynojirimycin, gluconolactone and glucose.

Cations, Divalent↗

Cell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p.

The role of glucose trimming in the endoplasmic reticulum of Saccharomyces cerevisiae was investigated using glucosidase inhibitors and mutant strains devoid of glucosidases I and II. These glucosidases are responsible for removing glucose residues from the N-linked core oligosaccharides attached to newly synthesized polypeptide chains. In mammalian cells they participate together with calnexin, calreticulin and UDP-glucose:glycoprotein glucosyltransferase in the folding and quality control of newly synthesized glycoproteins. In S.cerevisiae, glucosidase II is encoded by the GLS2 gene, and glucosidase I, as suggested here, by the CWH41 gene. Using castanospermine (an alpha-glucosidase inhibitor) and yeast strains defective in glucosidase I, glucosidase II and BiP/Kar2p, it was demonstrated that cell wall synthesis depends on the two glucosidases and BiP/Kar2p. In double mutants with defects in both BiP/Kar2p and either of the glucosidases the phenotype was particularly clear: synthesis of 1,6-beta-glucan_a cell wall component_was reduced; the cell wall displayed abnormal morphology; the cells aggregated; and their growth was severely inhibited. No defects in protein folding or secretion could be detected. We concluded that glucose trimming in S.cerevisiae is necessary for proper cell wall synthesis, and that the glucosidases function synergistically with BiP/Kar2p in this process.

Cell Wall↗

The bgl1 gene of Trichoderma reesei QM 9414 encodes an extracellular, cellulose-inducible beta-glucosidase involved in cellulase induction by sophorose.

We have investigated the effect of disruption of the bgl1-(beta-glucosidase l-encoding) gene of Trichoderma reesei on the formation of other beta-glucosidase activities and on the induction of cellulases. To this end the bgl1 locus was disrupted by insertion of the Aspergillus nidulans amdS (acetamidase-encoding) gene. The bgl1-disrupted strain did not produce the 75 kDa extracellular beta-glucosidase on cellulose or lactose, but still formed beta-glucosidase activity on glucose, cellobiose, xylan or beta-1,3-glucan, suggesting that the enzyme(s) exhibiting this beta-glucosidase activity is (are) not encoded by bgl1. The cellulase-inducer sophorose induced the bgl1-encoded beta-glucosidase, whereas the remaining beta-glucosidase activity was induced by methyl-beta-D-glucoside. The bgl1-gene product was mainly secreted into the medium, whereas the other beta-glucosidase activity was mainly associated with the cells. A bgl1-multicopy strain formed higher amounts of cellulases than the parent strain. Nonsaturating concentrations of sophorose efficiently induced cellobiohydrolase l formation in the bgl1-multicopy strain, but less efficiently in the bgl1-disrupted strain. The multicopy strain and the parent strain were comparably efficient at saturating sophorose concentrations. The beta-glucosidase inhibitor nojirimycin strongly inhibited induction in all strains. These data suggest that the bgl1-encoded beta-glucosidase is not identical to the plasma-membrane-bound, constitutive, methyl-beta-glucoside inducible beta-glucosidase, but represents an extracellular cellulose-induced enzyme. Both enzymes contribute to rapid induction of cellulases by modifying the inducer sophorose.

Base Sequence↗

Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene.

The gene coding for Bacillus cereus ATCC7064 (mesophile) oligo-1,6-glucosidase was cloned within a 2.8-kb SalI-EcoRI fragment of DNA, using the plasmid pUC19 as a vector and Escherichia coli C600 as a host. E. coli C600 bearing the hybrid plasmid pBCE4 accumulated oligo-1,6-glucosidase in the cytoplasm. The cloned enzyme coincided absolutely with B. cereus oligo-1,6-glucosidase in its Mr (65,000), in its electrophoretic behavior on a polyacrylamide gel with or without sodium dodecyl sulfate, in its isoelectric point (4.5), in the temperature dependence of its stability and activity, and in its antigenic determinants. The nucleotide sequence of B. cereus oligo-1,6-glucosidase gene and its flanking regions was determined with both complementary strands of DNA (each 2838 nucleotides). The gene consisted of an open reading frame of 1674 bp commencing with a ATG start codon and followed by a TAA stop codon. The amino acid sequence deduced from the nucleotide sequence predicted a protein of 558 amino acid residues with a Mr of 66,010. The amino acid composition and Mr were comparable with those of B. cereus oligo-1,6-glucosidase. The predicted N-terminal sequence of 10 amino acid residues agreed completely with that of the cloned ligo-1,6-glucosidase. The deduced amino acid sequence of B. cereus oligo-1,6-glucosidase was 72% and 42% similar to those from Bacillus thermoglucosidasius KP1006 (DSM2542, obligate thermophile) oligo-1,6-glucosidase and from Saccharomyces carlsbergensis CB11 alpha-glucosidase, respectively. Predictions of protein secondary structures along with amino acid sequence alignments demonstrated that B. cereus oligo-1,6-glucosidase may take the similar (alpha/beta)8-barrel super-secondary structure, a barrel of eight parallel beta-strands surrounded by eight alpha-helices, in its N-terminal active site domain as S. carlsbergensis alpha-glucosidase and Aspergillus oryzae alpha-amylase.

Amino Acid Sequence↗

Purification and properties of glucosidase I from mung bean seedlings.

The microsomal enzyme fraction from mung bean seedlings was found to contain glucosidase activity capable of releasing [3H]glucose from the glucose-labeled Glc3Man9GlcNAc. The enzymatic activity could be released in a soluble form by treating the microsomal particles with 1.5% Triton X-100. When the solubilized enzyme fraction was chromatographed on DE-52, it was possible to resolve glucosidase I activity (measured by the release of [3H]glucose from Glc3Man9GlcNAc) from glucosidase II (measured by release of [3H]glucose from Glc2Man9GlcNAc). The glucosidase I was purified about 200-fold by chromatography on hydroxylapatite, Sephadex G-200, dextran-Sepharose, and concanavalin A-Sepharose. The purified enzyme was free of glucosidase II and aryl-glucosidase activities. Only a single glucose residue could be released from the Glc3Man9GlcNAc by this purified enzyme and the other product was the Glc2Man9GlcNAc. Furthermore, this enzyme was inhibited in a dose-dependent manner by kojibiose, an alpha-1,2-linked glucose disaccharide, but not by other alpha-linked glucose disaccharides. These data indicate that this glucosidase is a specific alpha-1,2-glucosidase. The pH optimum for the glucosidase I was about 6.3 to 6.5, and no requirements for divalent cations were observed. The enzyme was inhibited strongly by the glucosidase processing inhibitors, castanospermine and deoxynojirimycin, and less strongly by the plant pyrrolidine alkaloid, 2,5-dihydroxymethyl-3,4-dihydroxypyrrolidine. However, the enzyme was not inhibited by the mannosidase processing inhibitors, swainsonine, deoxymannojirimycin or 1,4-dideoxy-1,4-imino-D-mannitol. The stability of the enzyme under various conditions and other properties of the enzyme were determined.

Chromatography↗

Isolation and characterization of a precursor form of lysosomal alpha-glucosidase from human urine.

A two-step procedure is described for the isolation of lysosomal alpha-glucosidase from human urine. In the second step, affinity chromatography on Sephadex G-100, two fractions with acid alpha-glucosidase activity were obtained. Fraction I contained alpha-glucosidase of Mr 109000, whereas fraction II contained components of Mr 76000 and 70000. alpha-Glucosidase in fraction I had an Mr similar to that of the precursor of alpha-glucosidase detected in the medium of fibroblasts after labelling with [14C]leucine. The components in fraction II had Mr identical to those of the mature forms of alpha-glucosidase found in placenta or cultured human skin fibroblasts. alpha-Glucosidase in fraction I contained mannose 6-phosphate (3.5 mol/mol polypeptide). No mannose 6-phosphate was present in the components in fraction II. Fraction I, but not fraction II, was avidly endocytosed by alpha-glucosidase-deficient cultured human skin fibroblasts. Endocytosis of fraction I was inhibited by mannose 6-phosphate. The pH optimum and Km values for p-nitrophenyl alpha-glucoside, maltose and glycogen of fractions I and II alpha-glucosidase were almost identical. However, the activity with glycogen relative to that of either p-nitrophenyl alpha-glucoside or maltose was lower in fraction I than in fraction II. It is concluded that fraction I consists of the precursor form of alpha-glucosidase and fraction II of the mature forms of the enzyme. The importance of urine as a source of precursors of lysosomal enzymes is discussed.

Adult↗

Classification of some alpha-glucosidases and alpha-xylosidases on the basis of substrate specificity.

Three alpha-glucosidases which passed under the names of transglucosidase (from Aspergillus niger), maltase (from Brewers yeast), and isomaltase (from Bakers yeast) for reasons of their substrate specificities and transfer actions, were purified to electrophoretically pure states. These purified alpha-glucosidases were made uniform in the hydrolyzing activities using p-nitrophenyl alpha-glucopyranoside (alpha-p-NPG) and were reacted with p-nitrophenyl alpha-xylopyranoside (alpha-p-NPX) or isoprimeverose (xylopyranosyl-alpha-1,6-glucopyranose), which are typical substrates of alpha-xylosidase. Only Asp. niger alpha-glucosidase among them hydrolyzed alpha-p-NPX and isoprimeverose. Further the substrate specificities of three alpha-glucosidases and two alpha-xylosidases (I and II from Asp. flavus MO-5) were investigated on maltose, isomaltose, alpha-p-NPG, isoprimeverose, and alpha-p-NPX in detail, and kinetic parameters [Km, Vmax, and molecular activity (Ko)] were estimated and compared with each other. In the comparison of kinetic parameters, Asp. niger alpha-glucosidase showed a broad specificity, that is, containing isoprimeverose in addition to maltose, isomaltose, and alpha-p-NPG. Though this enzyme barely hydrolyzed alpha-p-NPX too, the velocity was very slow. Though both yeast alpha-glucosidases barely hydrolyzed alpha-p-NPX or isoprimeverose too, these substrates were not good for yeast enzymes. On the other hand, two alpha-xylosidases showed narrow specificities, such that the substrates except for alpha-p-NPX and isoprimeverose were not hydrolyzed at all. The action on isoprimerose by Asp. niger alpha-glucosidase was completely the same as that on isomaltose at optimum pH, optimum temperature, inhibition pattern of hydrolyzing activity by 1-deoxynojirimycin, and transfer action pattern. Accordingly, we interpret these results as indicating that the hydrolyzations of isomaltose and isoprimeverose by Asp. niger alpha-glucosidase were catalyzed at the same active site. Asp. niger enzyme that has both alpha-glucosidase activity and alpha-xylosidase activity was shown to be classified in a middle position between alpha-glucosidase and alpha-xylosidase.

Aspergillus niger↗

Selective determination of the activities of neutral and acid alpha-glucosidase using discontinuous assays.

Most biological fluids contain both neutral and acid alpha-glucosidase. Optimal conditions were therefore developed for the selective determination of the activity of neutral and acid alpha-glucosidase, using 2-step, discontinuous assays. In the first step of the assay of neutral alpha-glucosidase, glucose was liberated from maltose (citrate-phosphate buffer, pH 6.8, 20 mmol/l maltose, 25 mmol/l turanose). Under these incubation conditions, turanose inhibited the residual activity of acid alpha-glucosidase almost completely without influencing the activity of neutral alpha-glucosidase. In the first step of the acid alpha-glucosidase assay, glucose was liberated from maltose (citrate-phosphate buffer, pH 3.8, 50 mmol/l maltose, 2 mol/l potassium chloride). Under these incubation conditions, potassium ions stimulate the activity of acid alpha-glucosidase and simultaneously inhibit almost completely the residual activity of neutral alpha-glucosidase. In the second step of the assay of neutral and acid alpha-glucosidase, the liberated glucose was measured by hexokinase/glucose-6-phosphate dehydrogenase. The effect of turanose and potassium ions on neutral and acid alpha-glucosidase from human urine was characterized.

Glucose↗

Subcellular distribution of acid alpha-glucosidase in fibroblasts and of antigenically cross-reactive material in Pompe's disease fibroblasts.

From fibroblasts of two cases of Pompe's disease (acid alpha-glucosidase deficiency), one of the childhood type (RH-SF-1) and one of the adult type (RH-SF-2), and normal fibroblasts, antigenically cross-reactive material and acid alpha-glucosidase were immunoprecipitated and analysed by immunoelectrotransfer blotting. The acid alpha-glucosidase and antigenically cross-reactive material (which reacts with antibody raised against normal acid alpha-glucosidase) revealed a precursor form of molecular weight 97,000 and two major components of 79,000 and 76,000. When monensin was added to the fibroblast culture, the two major components of normal acid alpha-glucosidase were decreased, whereas the large molecular weight precursor was increased. On the other hand, the 97,000 molecular weight component of cross-reactive material in the Pompe's fibroblasts (RH-SF-1 and RH-SF-2) was only slightly increased on monensin treatment. The fibroblasts were pulse-chase labelled with [2-H3] mannose and 32Pi. The cross-reactive material and acid alpha-glucosidase were precipitated with anti acid alpha-glucosidase antibody, and after sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), fluorography was performed. The radiolabel of 3H in the cross-reactive material of RH-SF-1 and -2 was weak, and 32P in the cross-reactive material of both fibroblasts was very weak when compared with those of the acid alpha-glucosidase. The radiolabel of 32P in the cross-reactive material of RH-SF-1 was extremely weak. Immunofluorescence histochemistry revealed a granular localization of acid alpha-glucosidase in the normal fibroblast cytoplasm, and a diffuse distribution of cross-reactive material in the cytoplasm of RH-SF-1 and -2. Immuno-electron microscopic examinations showed a normal acid alpha-glucosidase localization on the inner side of the lysosomal membrane and also diffusely in the lysosome; when treated with monensin, it was present on the trans part of the Golgi apparatus. Antigenically cross-reactive material, however, was found in the cytoplasm and endoplasmic reticulum. Some lysosomal localization was observed sporadically. Even after monensin treatment, it was not demonstrated on the Golgi apparatus.

Antigens↗

Oligo-1,6-glucosidase from a thermophile, Bacillus thermoglucosidasius KP1006, was efficiently produced by combinatorial expression of GroEL in Escherichia coli.

To improve the production of oligo-1,6-glucosidase from the obligately thermophilic Bacillus thermoglucosidasius KP1006 in Escherichia coli, the combined expression of oligo-1,6-glucosidase with various chaperone proteins of Hsp (heat-shock protein) 60 team proteins (GroES and GroEL) or Hsp70 team proteins (GrpE, DnaK and DnaJ) from the same thermophile was examined. This attempt was based on the facts that, (i) among glycosyl hydrolases of Family 13, bacillary oligo-1,6-glucosidases share highest homology with yeast alpha-glucosidase, and (ii) this yeast enzyme interacts with GroEL. In B. thermoglucosidasius Hsp60 team proteins, in particular, GroEL brought about a remarkable rise in expression of B. thermoglucosidasius oligo-1,6-glucosidase, while Hsp70 team proteins had no significant effect. The effect of B. thermoglucosidasius GroEL on oligo-1,6-glucosidase expression was supported by the finding that thermally inactivated B. thermoglucosidasius oligo-1,6-glucosidase was revived by B. thermoglucosidasius GroEL. Although the molecular mass of B. thermoglucosidasius oligo-1,6-glucosidase (66 kDa) exceeds the major range of substrates for GroEL proteins, the GroEL molecules probably recognized the alpha/beta motifs contained in the N-terminal domain and the subdomain of the oligo-1,6-glucosidase. Here we show that (i) the production of B. thermoglucosidasius oligo-1,6-glucosidase in E. coli was improved 3.8-fold by Hsp60 team proteins, (ii) the system can function for the expression of other glycosyl hydrolases of Family 13 that have defects in expression and (iii) the combinatorial expression of thermostable proteins with GroEL from the same thermophile in E. coli can increase the production of thermostable enzymes, preventing problems derived from differences in protein biogenesis.

Amino Acid Sequence↗