pubmed-article:99144 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:99144 | lifeskim:mentions | umls-concept:C0004591 | lld:lifeskim |
pubmed-article:99144 | lifeskim:mentions | umls-concept:C0017786 | lld:lifeskim |
pubmed-article:99144 | lifeskim:mentions | umls-concept:C0017787 | lld:lifeskim |
pubmed-article:99144 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:99144 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:99144 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:99144 | pubmed:dateCreated | 1978-10-27 | lld:pubmed |
pubmed-article:99144 | pubmed:abstractText | Bacillus megaterium N.C.T.C. no. 10342 exhibits glutamate synthetase (EC 2.6.1.53) and glutamate dehydrogenase (EC 1.4.1.4) activities. Concentrations of glutamate synthase were high when the bacteria were grown on 3mM-NH4Cl and low when they were grown on 100mM-NH4Cl, whereas glutamate dehydrogenase concentrations were higher when the bacteria were grown on 100mM-NH4Cl than on 3mM-NH4Cl. Glutamate synthase and glutamate dehydrogenase were purified to homogeneity from B. megaterium grown in 10mM-glucose/10mM-NH4Cl. The purified enzymes had mol.wts. 840000 and 270000 for glutamate synthase and glutamate dehydrogenase respectively. The Km values for substrates with NADPH and coenzyme were (glutamate synthase activity shown first) 9 micron and 360 micron for 2-oxoglutarate, 7.1 micron and 8.7 micron for NADPH, and 0.2 mM for glutamine and 22 mM for NH4Cl, similar values to those of enzymes from Escherichia coli. Glutamate synthase contained NH3-dependent activity (different from authentic glutamate dehydrogenase), which was enhanced 4-fold during treatment at pH 4.6 NH3-dependent activity was generally about 2% of the glutamine-dependent activity. Amidination of glutamate synthase by the bi-functional cross-linking reagent dimethyl suberimidate inactivated glutamine-dependent glutamate synthase activity, but increased NH3-dependent activity. A cross-linked structure of mol.wt. approx 200000 was the main product formed. | lld:pubmed |
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pubmed-article:99144 | pubmed:language | eng | lld:pubmed |
pubmed-article:99144 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:99144 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:99144 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:99144 | pubmed:month | Jul | lld:pubmed |
pubmed-article:99144 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:99144 | pubmed:author | pubmed-author:HemmiläI AIA | lld:pubmed |
pubmed-article:99144 | pubmed:author | pubmed-author:MäntsäläP IPI | lld:pubmed |
pubmed-article:99144 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:99144 | pubmed:day | 1 | lld:pubmed |
pubmed-article:99144 | pubmed:volume | 173 | lld:pubmed |
pubmed-article:99144 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:99144 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:99144 | pubmed:pagination | 45-52 | lld:pubmed |
pubmed-article:99144 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:99144 | pubmed:year | 1978 | lld:pubmed |
pubmed-article:99144 | pubmed:articleTitle | Purification and properties of glutamate synthase and glutamate dehydrogenase from Bacillus megaterium. | lld:pubmed |
pubmed-article:99144 | pubmed:publicationType | Journal Article | lld:pubmed |
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