RRC ID 33567
著者 Fujita Y, Ramaley R, Freese E.
タイトル Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis.
ジャーナル J Bacteriol
Abstract Late during sporulation, Bacillus subtilis produces glucose dehydrogenase (GlcDH; EC 1.1.1.47), which can react with D-glucose or 2-deoxy-D-glucose and can use nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP) as a cofactor. This enzyme is found mainly in the forespore compartment and is present in spores; it is probably made exclusively in the forespore. The properties of GlcDH were determined both in crude cell extracts and after purification. The enzyme is stable at pH 6.5 but labile at pH 8 or higher; the pH optimum of enzyme activity is 8. After inactivation at pH 8, the activity can be recovered in crude extracts, but not in solutions of the purified enzyme, by incubation with 3 M KCl and 5 mM NAD or NADP. As determined by gel filtration, enzymatically active GlcDH has a molecular weight of about 115,000 (if the enzyme is assumed to be globular). GlcDH is distinct from a catabolite-repressible inositol dehydrogenase (EC 1.1.1.18), which can also react with D-glucose, requires specifically NAD as a cofactor, and has an electrophoretic mobility different from that of GlcDH.
巻・号 132(1)
ページ 282-93
公開日 1977-10-1
DOI 10.1128/jb.132.1.282-293.1977
PMID 21162
PMC PMC221854
MeSH Bacillus subtilis / enzymology* Bacillus subtilis / growth & development Carbohydrate Dehydrogenases* / isolation & purification Cell-Free System Cytoplasm / enzymology Deoxyglucose / metabolism Enzyme Activation Glucose / metabolism Glucose Dehydrogenases* / isolation & purification Glucose Dehydrogenases* / metabolism Glucosephosphate Dehydrogenase / metabolism Hydrogen-Ion Concentration NAD / metabolism NADP / metabolism Spores, Bacterial / enzymology Spores, Bacterial / growth & development Subcellular Fractions
IF 3.006
リソース情報
原核生物(枯草菌) MBS67