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rdf:type |
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lifeskim:mentions |
umls-concept:C0014442,
umls-concept:C0037633,
umls-concept:C0043309,
umls-concept:C0204727,
umls-concept:C0205409,
umls-concept:C0205474,
umls-concept:C0315192,
umls-concept:C0439742,
umls-concept:C0596966,
umls-concept:C0871161,
umls-concept:C0917783,
umls-concept:C1382100,
umls-concept:C1979844
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pubmed:dateCreated |
1997-10-16
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pubmed:abstractText |
The alpha-1,4-D-glucan phosphorylase from gram-positive Corynebacterium callunae has been isolated and characterized. The enzyme is inducible approx. 2-fold by maltose, but remarkably not repressed by D-glucose. The phosphorylase is a homodimer with a stoichiometric content of the cofactor pyridoxal 5'-phosphate per 88-kDa protein subunit. The specificity constants (kcat/Km, glucan) in the directions of glucan synthesis and degradation are used for the classification of the enzyme as the first bacterial starch phosphorylase. A preference for large over small substrates is determined by variations in the apparent binding constants rather than catalytic-centre activities. The contribution of substrate chain length to binding energy is explained assuming two glucan binding sites in C. callunae phosphorylase: an oligosaccharide binding site composed of five subsites and a high-affinity polysaccharide site separated from the active site. A structural model of the molecular shape of the phosphorylase was obtained from small-angle solution X-ray scattering measurements. A flat, slightly elongated, ellipsoidal model with the three axes related to each other as 1:(0.87-0.95):0.43 showed scattering equivalence with the enzyme molecule. The model of C. callunae phosphorylase differs from the structurally well-characterized rabbit-muscle phosphorylase in size and axial dimensions.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-13782387,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-13876866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-1830850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-2182117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-2667896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-3005273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-3037809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-3155826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-3298211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-4865311,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-4928624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-5529205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-5529545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-5799132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-5799133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-6349688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-6416293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-6490773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-6639940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-6996565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-7068584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-7634071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-7727513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-7856850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-7905479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-791642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-8004173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-8254668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-8585615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-8639623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-8706700,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-9009262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-9145112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307027-942051
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
326 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
773-83
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1997
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pubmed:articleTitle |
alpha-1,4-D-glucan phosphorylase of gram-positive Corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution X-ray scattering.
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pubmed:affiliation |
Division of Biochemical Engineering, Institute of Food Technology, Universität für Bodenkultur (BOKU), Muthgasse 18, A-1190 Vienna, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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