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https://hdl.handle.net/2440/13424
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dc.contributor.author | Hrmova, M. | - |
dc.contributor.author | MacGregor, E. | - |
dc.contributor.author | Biely, P. | - |
dc.contributor.author | Stewart, R. | - |
dc.contributor.author | Fincher, G. | - |
dc.date.issued | 1998 | - |
dc.identifier.citation | Journal of Biological Chemistry, 1998; 273(18):11134-11143 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | http://hdl.handle.net/2440/13424 | - |
dc.description.abstract | A beta-glucosidase, designated isoenzyme betaII, from germinated barley (Hordeum vulgare L.) hydrolyzes aryl-beta-glucosides and shares a high level of amino acid sequence similarity with beta-glucosidases of diverse origin. It releases glucose from the non-reducing termini of cellodextrins with catalytic efficiency factors, kcat/Km, that increase approximately 9-fold as the degree of polymerization of these substrates increases from 2 to 6. Thus, the enzyme has a specificity and action pattern characteristic of both beta-glucosidases (EC 3.2.1.21) and the polysaccharide exohydrolase, (1,4)-beta-glucan glucohydrolase (EC 3.2.1.74). At high concentrations (100 mM) of 4-nitrophenyl beta-glucoside, beta-glucosidase isoenzyme betaII catalyzes glycosyl transfer reactions, which generate 4-nitrophenyl-beta-laminaribioside, -cellobioside, and -gentiobioside. Subsite mapping with cellooligosaccharides indicates that the barley beta-glucosidase isoenzyme betaII has six substrate-binding subsites, each of which binds an individual beta-glucosyl residue. Amino acid residues Glu181 and Glu391 are identified as the probable catalytic acid and catalytic nucleophile, respectively. The enzyme is a family 1 glycoside hydrolase that is likely to adopt a (beta/alpha)8 barrel fold and in which the catalytic amino acid residues appear to be located at the bottom of a funnel-shaped pocket in the enzyme. | - |
dc.language.iso | en | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.source.uri | http://dx.doi.org/10.1074/jbc.273.18.11134 | - |
dc.subject | Hordeum | - |
dc.subject | beta-Glucosidase | - |
dc.subject | Glucan 1,4-beta-Glucosidase | - |
dc.subject | Peptide Mapping | - |
dc.subject | Crystallography, X-Ray | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Substrate Specificity | - |
dc.subject | Kinetics | - |
dc.subject | Catalysis | - |
dc.subject | Models, Chemical | - |
dc.subject | Molecular Sequence Data | - |
dc.title | Substrate binding and catalytic mechanism of a barley b-D-glucosidase (1,4)-b-D-glucan exohydrolase | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1074/jbc.273.18.11134 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Hrmova, M. [0000-0002-3545-0605] | - |
Appears in Collections: | Agriculture, Food and Wine publications Aurora harvest 2 |
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