 cellulosic biomass . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: The strain produced the highest endoglucanase ( EG ) , cellobiohydrolase ( CBH ) and beta-glucosidase ( BGL ) activities of 0 . 0 , 0 . 0 and 0U/mg-protein , respectively , with rice straw as the carbon source . Score: 0.00 Title: Beta-glucosidase , exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlu0 . Journal: Biochem . J Year: 0000 Type: ARTICLE Literature: oryza Field: title Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: The bglu0 cDNA for a beta-glucosidase cloned from rice ( Oryza sativa L ) seedlings was expressed as a soluble and active protein in Escherichia coli and designated BGlu0 . This enzyme hydrolysed beta-0 , 0-linked oligosaccharides with increasing catalytic efficiency ( kcat/Km ) values as the DP ( degree of polymerization ) increased from 0 to 0 . In contrast , hydrolysis of beta-0 , 0-linked oligosaccharides decreased from DP 0 to 0 , and polymers with a DP greater than 0 were not hydrolysed . The enzyme also hydrolysed p -nitrophenyl beta-D-glycosides and some natural glucosides but with lower catalytic efficiency than beta-linked oligosaccharides . Pyridoxine 0-O-beta-D-glucoside was the most efficiently hydrolysed natural glycoside tested . BGlu0 also had high transglucosylation activity towards pyridoxine , producing pyridoxine 0-O-beta-D-glucopyranoside in the presence of the glucose donor p-nitrophenyl beta-D-glucoside . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: Beta-glucosidase , exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlu0 . Score: 0.00 Title: Purification , crystallization and preliminary X-ray analysis of rice BGlu0 beta-glucosidase with and without 0-deoxy-0-fluoro-beta-D-glucoside . Journal: Acta Crystallograph . Sect . F Struct . Biol . Cryst Commun . Year: 0000 Type: ARTICLE Literature: oryza Field: title Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: Rice ( Oryza sativa ) BGlu0 beta-glucosidase was expressed in Escherichia coli with N-terminal thioredoxin and hexahistidine tags and purified by immobilized metal-affinity chromatography ( IMAC ) . After removal of the N-terminal tags , cation-exchange and S-000 gel-filtration chromatography yielded a 00 kDa BGlu0 with >00% purity . The free enzyme and a complex with 0 , 0-dinitrophenyl-0-deoxy-0-fluoro-beta-D-glucopyranoside inhibitor were crystallized by microbatch and hanging-drop vapour diffusion . Small tetragonal crystals of BGlu0 with and without inhibitor grew in 00% ( w/v ) PEG 0000 with 0 . 0 M sodium cacodylate pH 0 . 0 and 0 . 0 M zinc acetate . Crystals of BGlu0 with inhibitor were streak-seeded into 00% ( w/v ) PEG MME 0000 , 0 . 0 M ammonium sulfate , 0 . 0 M MES pH 0 . 0 to yield larger crystals . Crystals with and without inhibitor diffracted to 0 . 00 and 0 . 00 angstroms resolution , respectively , and had isomorphous orthorhombic unit cells belonging to space group P0 ( 0 ) 0 ( 0 ) 0 ( 0 ) . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: Purification , crystallization and preliminary X-ray analysis of rice BGlu0 beta-glucosidase with and without 0-deoxy-0-fluoro-beta-D-glucoside . Score: 0.00 Title: Enzymatic synthesis of cello-oligosaccharides by rice BGlu0 { beta } -glucosidase glycosynthase mutants . Journal: Year: 0000 Type: ARTICLE Literature: oryza Field: title Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: Rice ( BGlu0 ) beta-glucosidase is a glycosyl hydrolase family 0 enzyme that acts as an exoglucanase on beta- ( 0 , 0 ) - and short beta- ( 0 , 0 ) -linked gluco-oligosaccharides . Mutations of BGlu0 beta-glucosidase at glutamate residue 000 of its natural precursor destroyed the enzymes catalytic activity , but the enzyme could be rescued in the presence of the anionic nucleophiles formate and azide , which verifies that this residue is the catalytic nucleophile . The catalytic activities of three candidate mutants , E000G , E000S , and E000A , in the presence of the nucleophiles were compared . The E000G mutant had approximately 00 and 0000-fold higher catalytic efficiency than E000A and E000S , respectively . All three mutants could catalyze the synthesis of mixed length oligosaccharides by transglucosylation , when alpha-glucosyl fluoride was used as donor and pNP-cellobioside as acceptor . The E000G mutant gave the fastest transglucosylation rate , which was approximately 0 and 00 fold faster than E000S and E000A , respectively , and gave yields of up to 00-00 % insoluble products with a donor : acceptor ratio of 0 : 0 . ( 00 ) C-NMR , methylation analysis and electrospray ionization mass spectrometry showed that the insoluble products were beta- ( 0 , 0 ) -linked oligomers with a degree of polymerization ( DP ) of 0 to at least 00 . The BGlu0 E000G glycosynthase was found to prefer longer chain length oligosaccharides that occupy at least three sugar residue binding subsites as acceptors for productive transglucosylation . This is the first report of a beta-glucansynthase derived from an exoglycosidase that can produce long chain cello-oligosaccharides , which likely reflects the extended oligosaccharide binding site of rice BGlu0 beta-glucosidase . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: Enzymatic synthesis of cello-oligosaccharides by rice BGlu0 { beta } -glucosidase glycosynthase mutants . Score: 0.00 Title: Structural insights into rice BGlu0 beta-glucosidase oligosaccharide hydrolysis and transglycosylation . Journal: J Mol Biol Year: 0000 Type: MEDLINE Literature: oryza Field: title Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: The structures of rice BGlu0 beta-glucosidase , a plant beta-glucosidase active in hydrolyzing cell wall-derived oligosaccharides , and its covalent intermediate with 0-deoxy-0-fluoroglucoside have been solved at 0 . 0 A and 0 . 00 A resolution , respectively . The structures were similar to the known structures of other glycosyl hydrolase family 0 ( GH0 ) beta-glucosidases , but showed several differences in the loops around the active site , which lead to an open active site with a narrow slot at the bottom , compatible with the hydrolysis of long beta-0 , 0-linked oligosaccharides . Though this active site structure is somewhat similar to that of the Paenibacillus polymyxa beta-glucosidase B , which hydrolyzes similar oligosaccharides , molecular docking studies indicate that the residues interacting with the substrate beyond the conserved -0 site are completely different , reflecting the independent evolution of plant and microbial GH0 exo-beta-glucanase/beta-glucosidases . The complex with the 0-fluoroglucoside included a glycerol molecule , which appears to be in a position to make a nucleophilic attack on the anomeric carbon in a transglycosylation reaction . The coordination of the hydroxyl groups suggests that sugars are positioned as acceptors for transglycosylation by their interactions with E000 , the catalytic acid/base , and Y000 , which is conserved in barley BGQ00/beta-II beta-glucosidase , that has oligosaccharide hydrolysis and transglycosylation activity similar to rice BGlu0 . As the rice and barley enzymes have different preferences for cellobiose and cellotriose , residues that appeared to interact with docked oligosaccharides were mutated to those of the barley enzyme to see if the relative activities of rice BGlu0 toward these substrates could be changed to those of BGQ00 . Although no single residue appeared to be responsible for these differences , I000 , N000 and N000 did appear to interact with the substrates . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: Structural insights into rice BGlu0 beta-glucosidase oligosaccharide hydrolysis and transglycosylation . Score: 0.00 Title: Expression of thermostable bacterial beta-glucosidase ( BglB ) in transgenic tobacco plants . Journal: Bioresour Technol Year: 0000 Type: MEDLINE Literature: oryza Field: title Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: Transgenic tobacco plants expressing the hyperthermostable beta-glucosidase BglB of Thermotoga maritima were generated with the goal of cost-effective production of the enzyme for the application in bioconversion of lignocellulosic biomass . The enzyme was targeted to the cytosol and chloroplasts , where it accumulated to level of 0 . 0% and 0 . 0% of total soluble protein , respectively . The optimal temperature and pH of the plant-expressed BglB was 00 degrees C and 0 . 0 , respectively . BglB activity was preserved in leaves after lyophilization , but decreased by over 00% with drying at room temperature . When BglB was synergistically supplied in a 0% ( w/v ) rice straw with Cel0A for efficient cellulase conversion , a 00% increase in glucose was observed . This report demonstrates the potential of utilizing transgenic tobacco for mass production of BglB . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: Expression of thermostable bacterial beta-glucosidase ( BglB ) in transgenic tobacco plants . Score: 0.00 Title: The structural basis of oligosaccharide binding by rice BGlu0 beta-glucosidase . Journal: J Struct Biol Year: 0000 Type: MEDLINE Literature: oryza Field: title Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: Rice BGlu0 beta-glucosidase is an oligosaccharide exoglucosidase that binds to six beta- ( 0-->0 ) -linked glucosyl residues in its active site cleft . Here , we demonstrate that a BGlu0 E000Q active site mutant can be effectively rescued by small nucleophiles , such as acetate , azide and ascorbate , for hydrolysis of aryl glycosides in a pH-independent manner above pH0 , consistent with the role of E000 as the catalytic acid-base . Cellotriose , cellotetraose , cellopentaose , cellohexaose and laminaribiose are not hydrolyzed by the mutant and instead exhibit competitive inhibition . The structures of the BGlu0 E000Q , its complexes with cellotetraose , cellopentaose and laminaribiose , and its covalent intermediate with 0-deoxy-0-fluoroglucoside were determined at 0 . 00 , 0 . 00 , 0 . 00 , 0 . 00 , and 0 . 00A resolution , respectively . The Q000Nepsilon was found to hydrogen bond to the glycosidic oxygen of the scissile bond , thereby explaining its high activity . The enzyme interacts with cellooligosaccharides through direct hydrogen bonds to the nonreducing terminal glucosyl residue . However , interaction with the other glucosyl residues is predominantly mediated through water molecules , with the exception of a direct hydrogen bond from N000 to glucosyl residue 0 , consistent with the apparent high binding energy at this residue . Hydrophobic interactions with the aromatic sidechain of W000 appear to orient glucosyl residues 0 and 0 , while Y000 orients glucosyl residues 0 and 0 . In contrast , laminaribiose has its second glucosyl residue positioned to allow direct hydrogen bonding between its O0 and Q000 Oepsilon and O0 and N000 . These are the first GH0 glycoside hydrolase family structures to show oligosaccharide binding in the hydrolytic configuration . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: The structural basis of oligosaccharide binding by rice BGlu0 beta-glucosidase . Score: 0.00 Title: QM/MM studies on the glycosylation mechanism of rice BGlu0 beta-glucosidase . Journal: J Mol Graph Model Year: 0000 Type: MEDLINE Literature: oryza Field: title Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: The quantum-mechanical/molecular-mechanical ( QM/MM ) method was used to study the glycosylation mechanism of rice BGlu0 beta-glucosidase in complex with laminaribiose . The calculation results reveal that the glycosylation step experiences a concerted process from the reactant to the glycosyl-enzyme complex with an activation barrier of 00 . 0 kcal/mol , in which an oxocarbenium cation-like transition state ( TS ) is formed . At the TS , the terminal saccharide residue planarizes toward the half-chair conformation , and the glycosidic bond cleavage is promoted by the attacks of proton donor ( E000 ) on glycosidic oxygen and nucleophilic residue ( E000 ) on the anomeric carbon of laminaribiose . Both the nucleophilic glutamate ( E000 ) and acid/base catalyst ( E000 ) establish shorter hydrogen bridges with the C-hydroxyl groups of sugar ring , which play an important role in the catalytic reaction of rice BGlu0 beta-glucosidase . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: QM/MM studies on the glycosylation mechanism of rice BGlu0 beta-glucosidase . Score: 0.00 Title: The rice bright green leaf ( bgl ) locus encodes OsRopGEF00 , which activates the development of small cuticular papillae on leaf surfaces . Journal: Plant Mol Biol Year: 0000 Type: MEDLINE Literature: oryza Field: title Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: Development of specialized epidermal cells and structures plays a key role in plant tolerance to biotic and abiotic stresses . In the paddy field , the bright green leaf ( bgl ) mutants of rice ( Oryza sativa ) exhibit a luminous green color that is clearly distinguishable from the normal green of wild-type plants . Transmission and scanning electron microscopy revealed that small cuticular papillae ( or small papillae ; SP ) , nipple-like structures , are absent on the adaxial and abaxial leaf surfaces of bgl mutants , leading to more direct reflection and less diffusion of green light . Map-based cloning revealed that the bgl locus encodes OsRopGEF00 , one of eleven OsRopGEFs in rice . RopGEFs ( guanine nucleotide exchange factors for Rop ) activate Rop/Rac GTPases , acting as molecular switches in eukaryotic signal transduction by replacing the bound GDP ( inactive form ) with GTP ( active form ) in response to external or internal cues . In agreement with the timing of SP initiation on the leaf epidermis , OsRopGEF00 is most strongly expressed in newly developing leaves before emergence from the leaf sheath . In yeast two-hybrid assays , OsRopGEF00 interacts with OsRac0 , one of seven OsRac proteins ; consistent with this , both proteins are localized in the plasma membrane . These results suggest that OsRopGEF00 activates OsRac0 to turn on the molecular signaling pathway for SP development . Together , our findings provide new insights into the molecular genetic mechanism of SP formation during early leaf morphogenesis . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: The rice bright green leaf ( bgl ) locus encodes OsRopGEF00 , which activates the development of small cuticular papillae on leaf surfaces . Score: 0.00 Title: Rice BGlu0 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition . Journal: Carbohydr Res Year: 0000 Type: MEDLINE Literature: oryza Field: title Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: The rice BGlu0 beta-D-glucosidase nucleophile mutant E000G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from alpha-d-glucopyranosyl fluoride ( GlcF ) donor and p-nitrophenyl ( pNP ) cellobioside ( Glc0-pNP ) or cello-oligosaccharide acceptors . When activity with other donors and acceptors was tested , the initial enzyme preparation cleaved pNP-beta-D-glucopyranoside ( Glc-pNP ) and pNP-beta-D-fucopyranoside ( Fuc-pNP ) to pNP and glucose and fucose , suggesting contamination with wild type BGlu0 beta-glucosidase . The products from reaction of GlcF and Fuc-pNP included Fuc-beta- ( 0-->0 ) -Fuc-pNP , Glc-beta- ( 0-->0 ) -Fuc-pNP , and Fuc-beta- ( 0-->0 ) -Glc-beta- ( 0-->0 ) -Fuc-pNP , suggesting the presence of both wild type BGlu0 and its glycosynthase . Inhibition of the BGlu0 beta-glucosidase activity within this preparation by cyclophellitol confirmed that the E000G glycosynthase preparation was contaminated with wild type BGlu0 . Rice BGlu0 E000G-0 , generated from a new construct designed to minimize back-mutation , showed glycosynthase activity without wild type hydrolytic or transglycosylation activity . E000G-0 catalyzed transfer of glycosyl residues from GlcF , alpha-L-arabinosyl fluoride , alpha-D-fucosyl fluoride , alpha-D-galactosyl fluoride , alpha-D-mannosyl fluoride , and alpha-D-xylosyl fluoride donors to Glc0-pNP acceptor . The synthetic products from the reactions of alpha-fucosyl fluoride and alpha-mannosyl fluoride donors were confirmed to result from addition of a beta- ( 0-->0 ) -linked glycosyl residue . Moreover , the E000G glycosynthase transferred glucose from GlcF donor to glucose , cellobiose , Glc-pNP , Fuc-pNP , pNP-beta-D-galactopyranoside , and pNP-beta-D-xylopyranoside acceptors , but little to pNP-beta-D-mannopyranoside . Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 0-OH . Elimination of wild type contamination thereby allowed a clear assessment of BGlu0 E000G glycosynthase catalytic abilities . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: Rice BGlu0 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition .