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glucosidase/oryza sativa
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Hydrolysis of Conjugated Gibberellins by β-Glucosidases from Dwarf Rice (Oryza sativa L. cv. «Tan-ginbozu»).
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Dwarf rice (Oryza sativa L. cv. «Tan-ginbozu») is widely used for gibberellin conjugate bioassay. Soluble and particulate fractions from seeds and seedlings of this variety showed hydrolytic activity toward [(3)H]GA-O-Glc. The soluble fraction from mature seeds exhibited the highest
Expression and enzymatic properties of rice (Oryza sativa L.) monolignol β-glucosidases.
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Monolignol glucosides and their β-glucosidases are found in monocots, but their biological roles are unclear. Phylogenetic analysis of rice (Oryza sativa L.) glycoside hydrolase family GH1 β-glucosidases indicated that Os4BGlu14, Os4BGlu16, and Os4BGlu18 are closely related to known monolignol
Multiple forms of alpha-glucosidase in rice seeds (Oryza sativa L., var Nipponbare).
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Two isoforms of alpha-glucosidases (ONG2-I and ONG2-II) were purified from dry rice seeds (Oryza sativa L., var Nipponbare). Both ONG2-I and ONG2-II were the gene products of ONG2 mRNA expressed in ripening seeds. Each enzyme consisted of two components of 6kDa-peptide and 88kDa-peptide encoded by
Expression, purification, crystallization and preliminary X-ray analysis of rice (Oryza sativa L.) Os4BGlu12 beta-glucosidase.
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Rice (Oryza sativa L.) Os4BGlu12, a glycoside hydrolase family 1 beta-glucosidase (EC 3.2.1.21), was expressed as a fusion protein with an N-terminal thioredoxin/His(6) tag in Escherichia coli strain Origami B (DE3) and purified with subsequent removal of the N-terminal tag. Native Os4BGlu12 and its
A stress-induced rice (Oryza sativa L.) beta-glucosidase represents a new subfamily of glycosyl hydrolase family 5 containing a fascin-like domain.
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GH5BG, the cDNA for a stress-induced GH5 (glycosyl hydrolase family 5) beta-glucosidase, was cloned from rice (Oryza sativa L.) seedlings. The GH5BG cDNA encodes a 510-amino-acid precursor protein that comprises 19 amino acids of prepeptide and 491 amino acids of mature protein. The protein was
The crystal structure of rice (Oryza sativa L.) Os4BGlu12, an oligosaccharide and tuberonic acid glucoside-hydrolyzing β-glucosidase with significant thioglucohydrolase activity.
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Rice Os4BGlu12, a glycoside hydrolase family 1 (GH1) β-glucosidase, hydrolyzes β-(1,4)-linked oligosaccharides of 3-6 glucosyl residues and the β-(1,3)-linked disaccharide laminaribiose, as well as certain glycosides. The crystal structures of apo Os4BGlu12, and its complexes with
Identification of a beta-glucosidase hydrolyzing tuberonic acid glucoside in rice (Oryza sativa L.).
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Tuberonic acid (TA) and its glucoside (TAG) have been isolated from potato (Solanum tuberosum L.) leaflets and shown to exhibit tuber-inducing properties. These compounds were reported to be biosynthesized from jasmonic acid (JA) by hydroxylation and subsequent glycosylation, and to be contained in
In silico molecular modelling, structural dynamics simulation and characterization of antifungal nature of β-glucosidase enzyme from Sechium edule
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β-glucosidase is an enzyme that has ability to cleave β-glycosidic bonds present in oligosaccharides and glycoconjugates. They are known to be present across all domains of living organism and have important roles in many biological processes including plant defense mechanism. In the present study,
OsMOGS is required for N-glycan formation and auxin-mediated root development in rice (Oryza sativa L.).
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N-glycosylation is a major modification of glycoproteins in eukaryotic cells. In Arabidopsis, great progress has been made in functional analysis of N-glycan production, however there are few studies in monocotyledons. Here, we characterized a rice (Oryza sativa L.) osmogs mutant with shortened
Identification of rice β-glucosidase with high hydrolytic activity towards salicylic acid β-D-glucoside.
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β-Glucosidases (EC 3.2.1.21) split β-glucosidic linkages at the non-reducing end of glucosides and oligosaccharides to release β-D-glucose. One of the important functions of plant β-glucosidase is deglucosylation of inactive glucosides of phytohormones to regulate levels of active hormones.
Cloning and characterization of drought responsive partial gene sequence(s) from Oryza sativa L. subsp. Indica.
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Differential display gels were run for the drought tolerant (N-22) and drought susceptible (Panidhan) genotypes of rice (Oryza sativa) to identify the genes showing differential expression with respect to moisture stress. Differential cDNA products were cloned in PCR-Trap vector and analyzed for
Purification, crystallization and preliminary X-ray analysis of rice BGlu1 beta-glucosidase with and without 2-deoxy-2-fluoro-beta-D-glucoside.
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Rice (Oryza sativa) BGlu1 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-200 gel-filtration chromatography yielded a 50
Beta-glucosidase, exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlu1.
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The bglu1 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 BGlu1. This enzyme hydrolysed beta-1,4-linked oligosaccharides with increasing catalytic efficiency (kcat/Km) values as the DP (degree
Upregulation of jasmonate-inducible defense proteins and differential colonization of roots of Oryza sativa cultivars with the endophyte Azoarcus sp.
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The endophyte Azoarcus sp. strain BH72 expresses nitrogenase (nif) genes inside rice roots. We applied a proteomic approach to dissect responses of rice roots toward bacterial colonization and jasmonic acid (JA) treatment. Two sister lineages of Oryza sativa were analyzed with cv. IR42 showing a
Purification and characterization of rice alpha-glucosidase, a key enzyme for alcohol fermentation of rice polish.
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Alpha-glucosidase, a key enzyme for nuka-sake brewing, was purified from Oryza sativa cv. Yamadanishiki, which is widely used for sake brewing. The molecular weight of the purified enzyme was 95 kDa. The optimum pH and temperature were 4.5 and 55 degrees C, respectively. The substrate specificity
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