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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1994-3-10
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pubmed:abstractText |
It was verified, by n.m.r. and fast-atom-bombardment-m.s. studies, that the C-2 position of 1,5-anhydro-D-fructose, which was prepared by the reaction of immobilized glucose 2-oxidase from Coriolus versicolor (with 1,5-anhydro-D-glucitol), is hydrated to the acetal form in water. The effects of 1,5-anhydro-D-fructose on several glucose-metabolizing enzymes were compared with those of 1,5-anhydro-D-glucitol. Glucose 1-oxidase from Aspergillus niger was inhibited by 1,5-anhydro-D-fructose (Ki 6.6 mM) more effectively than 1,5-anhydro-D-glucitol (Ki 82.5 mM). Yeast and rat brain hexokinases phosphorylated 1,5-anhydro-D-fructose (Km,yeast 2.3 mM: Km,rat 0.79 mM) and 1,5-anhydro-D-glucitol (Km,yeast 3.9 mM; Km,rat 0.83 mM). The phosphorylated forms of these compounds inhibited D-glucose phosphorylation by yeast hexokinase (Ki of phosphorylated 1,5-anhydro-D-fructose 0.11 mM; Ki of phosphorylated 1,5-anhydro-D-glucitol 0.38 mM) and rat brain hexokinase (Ki of phosphorylated 1,5-anhydro-D-fructose 0.07 mM; Ki of phosphorylated 1,5-anhydro-D-glucitol 0.04 mM). Glucokinase phosphorylated neither 1,5-anhydro-D-fructose nor 1,5-anhydro-D-glucitol, and the phosphorylation of D-glucose by glucokinase was inhibited by them. Mutarotase was slightly inhibited by 1,5-anhydro-D-fructose, as well as by 1,5-anhydro-D-glucitol.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1,5-anhydrofructose,
http://linkedlifedata.com/resource/pubmed/chemical/1,5-anhydroglucitol,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrate Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrate Epimerases,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyglucose,
http://linkedlifedata.com/resource/pubmed/chemical/Fructose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucokinase,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Hexokinase,
http://linkedlifedata.com/resource/pubmed/chemical/aldose 1-epimerase,
http://linkedlifedata.com/resource/pubmed/chemical/pyranose oxidase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0885-4513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
18 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
275-83
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pubmed:dateRevised |
2007-3-21
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pubmed:meshHeading |
pubmed-meshheading:8297506-Aspergillus niger,
pubmed-meshheading:8297506-Carbohydrate Dehydrogenases,
pubmed-meshheading:8297506-Carbohydrate Epimerases,
pubmed-meshheading:8297506-Deoxyglucose,
pubmed-meshheading:8297506-Fructose,
pubmed-meshheading:8297506-Glucokinase,
pubmed-meshheading:8297506-Glucose,
pubmed-meshheading:8297506-Hexokinase,
pubmed-meshheading:8297506-Hydrolysis,
pubmed-meshheading:8297506-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8297506-Phosphorylation,
pubmed-meshheading:8297506-Spectrometry, Mass, Fast Atom Bombardment
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pubmed:year |
1993
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pubmed:articleTitle |
Effects of 1,5-anhydro-D-fructose on selected glucose-metabolizing enzymes.
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pubmed:affiliation |
Department of Clinical Biochemistry, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
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pubmed:publicationType |
Journal Article
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