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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
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pubmed:dateCreated |
1991-12-26
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pubmed:abstractText |
Two electrophoretically distinct proteins with fructokinase (ATP:fructose-6-phosphotransferase) activity were detected in Lactococcus lactis subsp. lactis K1. Whereas fructokinase I was induced specifically by growth of the organism on sucrose, fructokinase II was derepressed during growth on ribose, galactose, maltose, and lactulose. Fructokinase I was purified about 1000-fold to electrophoretic homogeneity (specific activity 112 units/mg). The amino acid composition, N-terminal sequence, nucleoside triphosphate, and metal requirement(s) of the enzyme are reported. Ultracentrifugal analysis showed that the enzyme was primarily dimeric with subunits of 33.5 kDa (+/- 5%). When completely reduced, fructokinase I migrated as a single protein (Mr = 32,000) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, but in the absence of reducing agent two polypeptides (apparent Mr = 29,000 and 31,000) were detected. Isoelectric focusing also revealed two polypeptides (pI 5.6 and 5.8), and both species catalyzed the phosphorylation of fructose and mannose. Hybridization studies showed that: (i) a sucrose-negative mutant lacking the fructokinase I gene (scrK) retained fructokinase II activity and (ii) scrK is closely linked to scrA and scrB which encode Enzyme IIScr and sucrose-6-phosphate hydrolase, respectively. In L. lactis K1, these genes and the N5-(1-carboxyethyl)-L-ornithine synthase gene (ceo) are encoded on the sucrose-nisin transposon Tn5306 in the order ceo-scrKAB.
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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/DNA Transposable Elements,
http://linkedlifedata.com/resource/pubmed/chemical/Fructokinases,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Sucrose,
http://linkedlifedata.com/resource/pubmed/chemical/fructokinase
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
266
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pubmed:geneSymbol |
scrK
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
22626-33
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:1658003-Carbohydrate Metabolism,
pubmed-meshheading:1658003-Chromatography, Affinity,
pubmed-meshheading:1658003-Chromatography, Gel,
pubmed-meshheading:1658003-Chromatography, Ion Exchange,
pubmed-meshheading:1658003-DNA Transposable Elements,
pubmed-meshheading:1658003-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1658003-Fructokinases,
pubmed-meshheading:1658003-Genes, Bacterial,
pubmed-meshheading:1658003-Isoenzymes,
pubmed-meshheading:1658003-Kinetics,
pubmed-meshheading:1658003-Lactococcus lactis,
pubmed-meshheading:1658003-Macromolecular Substances,
pubmed-meshheading:1658003-Molecular Weight,
pubmed-meshheading:1658003-Protein Conformation,
pubmed-meshheading:1658003-Restriction Mapping,
pubmed-meshheading:1658003-Sucrose
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pubmed:year |
1991
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pubmed:articleTitle |
Purification and properties of fructokinase I from Lactococcus lactis. Localization of scrK on the sucrose-nisin transposon Tn5306.
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pubmed:affiliation |
Laboratory of Microbial Ecology, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article
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