3ptk › Citations

The crystal structure of rice (Oryza sativa L.) Os4BGlu12, an oligosaccharide and tuberonic acid glucoside-hydrolyzing β-glucosidase with significant thioglucohydrolase activity.

Sansenya S, Opassiri R, Kuaprasert B, Chen CJ, Cairns JR
Arch Biochem Biophys 510 62-72 (2011)
Related entries: 3ptm, 3ptq

Cited: 15 times
EuropePMC logo PMID: 21521631

Abstract

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 2,4-dinitrophenyl-2-deoxyl-2-fluoroglucoside (DNP2FG) and 2-deoxy-2-fluoroglucose (G2F) were solved at 2.50, 2.45 and 2.40Å resolution, respectively. The overall structure of rice Os4BGlu12 is typical of GH1 enzymes, but it contains an extra disulfide bridge in the loop B region. The glucose ring of the G2F in the covalent intermediate was found in a (4)C(1) chair conformation, while that of the noncovalently bound DNP2FG had a (1)S(3) skew boat, consistent with hydrolysis via a (4)H(3) half-chair transition state. The position of the catalytic nucleophile (Glu393) in the G2F structure was more similar to that of the Sinapsis alba myrosinase G2F complex than to that in covalent intermediates of other O-glucosidases, such as rice Os3BGlu6 and Os3BGlu7 β-glucosidases. This correlated with a significant thioglucosidase activity for Os4BGlu12, although with 200- to 1200-fold lower k(cat)/K(m) values for S-glucosides than the comparable O-glucosides, while hydrolysis of S-glucosides was undetectable for Os3BGlu6 and Os3BGlu7.

Articles - 3ptk mentioned but not cited (4)

  1. Functional Characterization of CsBGlu12, a β-Glucosidase from Crocus sativus, Provides Insights into Its Role in Abiotic Stress through Accumulation of Antioxidant Flavonols. Baba SA, Vishwakarma RA, Ashraf N. J Biol Chem 292 4700-4713 (2017)
  2. Structure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase. Fiebig D, Schmelz S, Zindel S, Ehret V, Beck J, Ebenig A, Ehret M, Fröls S, Pfeifer F, Kolmar H, Fuchsbauer HL, Scrima A. J Biol Chem 291 20417-20426 (2016)
  3. Biochemical and Structural Analysis of a Glucose-Tolerant β-Glucosidase from the Hemicellulose-Degrading Thermoanaerobacterium saccharolyticum. Kim IJ, Bornscheuer UT, Nam KH. Molecules 27 290 (2022)
  4. In silico molecular modelling, structural dynamics simulation and characterization of antifungal nature of β-glucosidase enzyme from Sechium edule. Pathaw N, Gurung AB, Chrungoo NK, Bhattacharjee A, Roy SS, Ansari MA, Sharma SK. J Biomol Struct Dyn 39 4501-4509 (2021)


Articles citing this publication (11)

  1. Expression of the β-glucosidase gene Pgβglu-1 underpins natural resistance of white spruce against spruce budworm. Mageroy MH, Parent G, Germanos G, Giguère I, Delvas N, Maaroufi H, Bauce É, Bohlmann J, Mackay JJ. Plant J 81 68-80 (2015)
  2. Identification of the acid/base catalyst of a glycoside hydrolase family 3 (GH3) beta-glucosidase from Aspergillus niger ASKU28. Thongpoo P, McKee LS, Araújo AC, Kongsaeree PT, Brumer H. Biochim Biophys Acta 1830 2739-2749 (2013)
  3. Lotus japonicus flowers are defended by a cyanogenic β-glucosidase with highly restricted expression to essential reproductive organs. Lai D, Pičmanová M, Abou Hachem M, Motawia MS, Olsen CE, Møller BL, Rook F, Takos AM. Plant Mol Biol 89 21-34 (2015)
  4. Engineering the cytokinin-glucoside specificity of the maize β-D-glucosidase Zm-p60.1 using site-directed random mutagenesis. Filipi T, Mazura P, Janda L, Kiran NS, Brzobohatý B. Phytochemistry 74 40-48 (2012)
  5. Enzymatic and structural characterization of hydrolysis of gibberellin A4 glucosyl ester by a rice β-D-glucosidase. Hua Y, Sansenya S, Saetang C, Wakuta S, Ketudat Cairns JR. Arch Biochem Biophys 537 39-48 (2013)
  6. The evolutionary appearance of non-cyanogenic hydroxynitrile glucosides in the Lotus genus is accompanied by the substrate specialization of paralogous β-glucosidases resulting from a crucial amino acid substitution. Lai D, Abou Hachem M, Robson F, Olsen CE, Wang TL, Møller BL, Takos AM, Rook F. Plant J 79 299-311 (2014)
  7. A Computational Method to Propose Mutations in Enzymes Based on Structural Signature Variation (SSV). Mariano DCB, Santos LH, Machado KDS, Werhli AV, de Lima LHF, de Melo-Minardi RC. Int J Mol Sci 20 E333 (2019)
  8. Identification of rice Os4BGlu13 as a β-glucosidase which hydrolyzes gibberellin A4 1-O-β-d-glucosyl ester, in addition to tuberonic acid glucoside and salicylic acid derivative glucosides. Hua Y, Ekkhara W, Sansenya S, Srisomsap C, Roytrakul S, Saburi W, Takeda R, Matsuura H, Mori H, Ketudat Cairns JR. Arch Biochem Biophys 583 36-46 (2015)
  9. Structural analysis and insights into the glycon specificity of the rice GH1 Os7BGlu26 β-D-mannosidase. Tankrathok A, Iglesias-Fernández J, Luang S, Robinson RC, Kimura A, Rovira C, Hrmova M, Ketudat Cairns JR. Acta Crystallogr D Biol Crystallogr 69 2124-2135 (2013)
  10. Molecular cloning, characterization and in silico analysis of a thermostable β-glucosidase enzyme from Putranjiva roxburghii with a significant activity for cellobiose. Kar B, Verma P, Patel GK, Sharma AK. Phytochemistry 140 151-165 (2017)
  11. Structural analysis of rice Os4BGlu18 monolignol β-glucosidase. Baiya S, Pengthaisong S, Kitjaruwankul S, Ketudat Cairns JR. PLoS One 16 e0241325 (2021)


Quick links