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https://hdl.handle.net/2440/145
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dc.contributor.author | Lee, R. | - |
dc.contributor.author | Hrmova, M. | - |
dc.contributor.author | Burton, R. | - |
dc.contributor.author | Lahnstein, J. | - |
dc.contributor.author | Fincher, G. | - |
dc.date.issued | 2003 | - |
dc.identifier.citation | Journal of Biological Chemistry, 2003; 278(7):5377-5387 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | http://hdl.handle.net/2440/145 | - |
dc.description.abstract | An alpha-l-arabinofuranosidase and a beta-d-xylosidase, designated ARA-I and XYL, respectively, have been purified about 1,000-fold from extracts of 5-day-old barley (Hordeum vulgare L.) seedlings using ammonium sulfate fractional precipitation, ion exchange chromatography, chromatofocusing, and size-exclusion chromatography. The ARA-I has an apparent molecular mass of 67 kDa and an isoelectric point of 5.5, and its catalytic efficiency during hydrolysis of 4'-nitrophenyl alpha-l-arabinofuranoside is only slightly higher than during hydrolysis of 4'-nitrophenyl beta-d-xyloside. Thus, the enzyme is actually a bifunctional alpha-l-arabinofuranosidase/beta-d-xylosidase. In contrast, the XYL enzyme, which also has an apparent molecular mass of 67 kDa and an isoelectric point of 6.7, preferentially hydrolyzes 4'-nitrophenyl beta-d-xyloside, with a catalytic efficiency approximately 30-fold higher than with 4'-nitrophenyl alpha-l-arabinofuranoside. The enzymes hydrolyze wheat flour arabinoxylan slowly but rapidly hydrolyze oligosaccharide products released from this polysaccharide by (1 --> 4)-beta-d-xylan endohydrolase. Both enzymes hydrolyze (1 --> 4)-beta-d-xylopentaose, and ARA-I can also degrade (1 --> 5)-alpha-l-arabinofuranohexaose. ARA-I and XYL cDNAs encode mature proteins of 748 amino acid residues which have calculated molecular masses of 79.2 and 80.5 kDa, respectively. Both are family 3 glycoside hydrolases. The discrepancies between the apparent molecular masses obtained for the purified enzymes and those predicted from the cDNAs are attributable to COOH-terminal processing, through which about 130 amino acid residues are removed from the primary translation product. The genes encoding the ARA-I and XYL have been mapped to chromosomes 2H and 6H, respectively. ARA-I transcripts are most abundant in young roots, young leaves, and developing grain, whereas XYL mRNA is detected in most barley tissues. | - |
dc.description.statementofresponsibility | Robert C Lee, Maria Hrmova, Rachel A Burton, Jelle Lahnstein, Geoffrey B Fincher | - |
dc.language.iso | en | - |
dc.publisher | Amer Soc Biochemistry Molecular Biology Inc | - |
dc.source.uri | http://dx.doi.org/10.1074/jbc.m210627200 | - |
dc.subject | Hordeum | - |
dc.subject | Glycoside Hydrolases | - |
dc.subject | Xylosidases | - |
dc.subject | Plant Proteins | - |
dc.subject | Sequence Alignment | - |
dc.subject | Protein Processing, Post-Translational | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Substrate Specificity | - |
dc.subject | Hydrolysis | - |
dc.subject | Molecular Sequence Data | - |
dc.title | Bifunctional family 3 glycoside hydrolases from barley with alpha-L-arabinofuranosidase and beta-D-xylosidase activity - Characterization, primary structures, and COOH-terminal processing | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1074/jbc.M210627200 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Hrmova, M. [0000-0002-3545-0605] | - |
dc.identifier.orcid | Burton, R. [0000-0002-0638-4709] | - |
dc.identifier.orcid | Lahnstein, J. [0000-0002-4202-1403] | - |
Appears in Collections: | Agriculture, Food and Wine publications Aurora harvest 2 |
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