{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T20:49:14Z","timestamp":1761598154525},"reference-count":22,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[1977,10,1]],"date-time":"1977-10-01T00:00:00Z","timestamp":244512000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[1977,10]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1128\/jb.132.1.282-293.1977","type":"journal-article","created":{"date-parts":[[2020,1,3]],"date-time":"2020-01-03T16:18:12Z","timestamp":1578068292000},"page":"282-293","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":89,"title":["Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis"],"prefix":"10.1128","volume":"132","author":[{"given":"Y","family":"Fujita","sequence":"first","affiliation":[]},{"given":"R","family":"Ramaley","sequence":"additional","affiliation":[]},{"given":"E","family":"Freese","sequence":"additional","affiliation":[]}],"member":"235","reference":[{"key":"p_1","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1128\/JB.83.4.699-707.1962","article-title":"Aerobic sporulating bacteria. I. Glucose dehydrogenase ofBacillus cereus","volume":"83","author":"Bach J. A.","year":"1962","unstructured":"Bach , J. A. , and H. L. Sadoff . 1962 . Aerobic sporulating bacteria. I. Glucose dehydrogenase ofBacillus cereus . J. Bacteriol. 83 : 699 - 707 .","journal-title":"J. Bacteriol."},{"key":"p_2","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1128\/jb.108.2.720-732.1971","article-title":"Acrylamide gel electrophoresis of intracellular proteins during early stages ofsporulation in Bacillus subtilis","volume":"108","author":"Bott K. F.","year":"1971","unstructured":"Bott , K. F. 1971 . Acrylamide gel electrophoresis of intracellular proteins during early stages ofsporulation in Bacillus subtilis . J. Bacteriol. 108 : 720 - 732 .","journal-title":"J. Bacteriol."},{"key":"p_3","doi-asserted-by":"crossref","unstructured":"Chrambach A. T. M. Jovin P. J. Svendsen and D. Rodbard. 1976. Analytical and preparative polyacrylamide gel electrophoresis: an objectively defined fractionation route apparatus and procedures. In N. Catsimpoolas (ed.) Methods of protein separation: a modern survey. Plenum Press New York.","DOI":"10.1007\/978-1-4684-9984-1_2"},{"key":"p_4","unstructured":"Freese E. and Y. Fujita. 1976. Control of enzyme synthesis during growth and sporulation p. 164-184. In D. Schlessinger (ed.) Microbiology -1976. American Society for Microbiology Washington D.C."},{"key":"p_5","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0304-4165(70)90115-7","article-title":"Commitment to sporulation and induction of glucose-phosphoenolpyruvatetransferase","volume":"222","author":"Freese E.","year":"1970","unstructured":"Freese , E. , W. Klofat , and E. Galliers . 1970 . Commitment to sporulation and induction of glucose-phosphoenolpyruvatetransferase . Biochim. Biophys. Acta 222 : 265 - 289 .","journal-title":"Biochim. Biophys. Acta"},{"key":"p_6","doi-asserted-by":"crossref","first-page":"1046","DOI":"10.1128\/JB.101.3.1046-1062.1970","article-title":"Growth, sporulation, and enzyme defects of glucosamine mutants of Bacillus subtilis","volume":"101","author":"Freese E. B.","year":"1970","unstructured":"Freese , E. B. , R. M. Cole , W. Klofat , and E. Freese . 1970 . Growth, sporulation, and enzyme defects of glucosamine mutants of Bacillus subtilis . J. Bacteriol. 101 : 1046 - 1062 .","journal-title":"J. Bacteriol."},{"key":"p_7","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1128\/jb.107.2.442-447.1971","article-title":"Reactivation action of ethylenediaminetetraacetic acid or dipicolinic acid on inactive glucose dehydrogenase obtained from heated spores of Bacillus subtilis","volume":"107","author":"Hachisuka Y.","year":"1971","unstructured":"Hachisuka , Y. , and K. Tochikubo . 1971 . Reactivation action of ethylenediaminetetraacetic acid or dipicolinic acid on inactive glucose dehydrogenase obtained from heated spores of Bacillus subtilis . J. Bacteriol. 107 : 442 - 447 .","journal-title":"J. Bacteriol."},{"key":"p_8","unstructured":"Jovin T. M. M. L. Dante and A. Chrambach. 1970. Multiphase buffer systems output (PB196085-196091). National Technical Service Springfield Va."},{"key":"p_9","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","article-title":"Protein measurement with the Folin phenol reagent","volume":"193","author":"Lowry 0.","year":"1951","unstructured":"Lowry , 0. H. , N. J. Rosebrough , A. L. Farr , and R. J. Randall . 1951 . Protein measurement with the Folin phenol reagent . J. Biol. Chem. 193 : 265 - 275 .","journal-title":"J. Biol. Chem."},{"key":"p_10","unstructured":"McCormick N. G. F. Feeherry and H. S. Levinson. 1972. Germination properties and proteins of spores of Bacillus megaterium. QM B1551 mutants p. 421-429. In H. 0. Halvorson R. Hanson and L. L. Campbell (ed.) Spores V. American Society for Microbiology Washington D.C."},{"key":"p_11","doi-asserted-by":"crossref","first-page":"1613","DOI":"10.1515\/bchm2.1975.356.2.1613","article-title":"D-glucose dehydrogenase from Bacillus megaterium M1286: purification, properties and structure","volume":"356","author":"Pauly H. E.","year":"1975","unstructured":"Pauly , H. E. , and G. Pfleiderer . 1975 . D-glucose dehydrogenase from Bacillus megaterium M1286: purification, properties and structure . Hoppe-Seyler's Z. Physiol. Chem. 356 : 1613 - 1623 .","journal-title":"Hoppe-Seyler's Z. Physiol. Chem."},{"key":"p_12","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1128\/br.40.4.908-962.1976","article-title":"Genetic aspects of bacterial endospore formation","volume":"40","author":"Piggot P. G.","year":"1976","unstructured":"Piggot , P. G. , and J. G. Coote . 1976 . Genetic aspects of bacterial endospore formation . Bacteriol. Rev. 40 : 908 - 962 .","journal-title":"Bacteriol. Rev."},{"key":"p_13","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1128\/jb.119.3.805-810.1974","article-title":"Initiation of spore germination in Bacillus subtilis: relationship to inhibition of L-alanine metabolism","volume":"119","author":"Prasad C.","year":"1974","unstructured":"Prasad , C. 1974 . Initiation of spore germination in Bacillus subtilis: relationship to inhibition of L-alanine metabolism . J. Bacteriol. 119 : 805 - 810 .","journal-title":"J. Bacteriol."},{"key":"p_14","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1128\/jb.110.1.321-328.1972","article-title":"Initiation of spore germination in glycolytic mutants of Bacillus subtilis","volume":"110","author":"Prasad C.","year":"1972","unstructured":"Prasad , C. , M. Diesterhaft , and E. Freese . 1972 . Initiation of spore germination in glycolytic mutants of Bacillus subtilis . J. Bacteriol. 110 : 321 - 328 .","journal-title":"J. Bacteriol."},{"key":"p_15","first-page":"40","article-title":"ttude morphological de la sporulation de Bacillus subtilis","volume":"108","author":"Ryter A.","year":"1965","unstructured":"Ryter , A. 1965 . ttude morphological de la sporulation de Bacillus subtilis . Ann. Inst. Pasteur (Paris) 108 : 40 - 60 .","journal-title":"Ann. Inst. Pasteur (Paris)"},{"key":"p_16","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0076-6879(66)09026-8","article-title":"Glucose dehydrogenases-soluble","volume":"9","author":"Sadoff H. L.","year":"1966","unstructured":"Sadoff , H. L. 1966 . Glucose dehydrogenases-soluble . Methods Enzymol. 9 : 103 - 111 .","journal-title":"Methods Enzymol."},{"key":"p_17","unstructured":"Sadoff H. L. J. A. Bach and J. W. Kools. 1965. Significance of multiple forms of glucose dehydrogenase in relation to its heat resistance p. 97-110. In L. L. Campbell and H. 0. Halvorson (ed.) Spores III. American Society for Microbiology Ann Arbor Mich."},{"key":"p_18","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1073\/pnas.70.3.778","article-title":"Hydrophobic chromatography use for purification of glycogen synthetase","volume":"70","author":"Shaltiel S.","year":"1973","unstructured":"Shaltiel , S. , and Z. Er -el. 1973 . Hydrophobic chromatography use for purification of glycogen synthetase . Proc. Natl. Acad. Sci. U.S.A. 70 : 778 - 781 .","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"p_19","unstructured":"Thorley C. M. and J. Wolf. 1961. Some germination factors of mesophilia spore formers p. 1-23. In H. 0. Halvorson (ed.) Spore II. Burgess Publishing Co. Minneapolis."},{"key":"p_20","first-page":"101","article-title":"Eine Glucose-Dehydrogenase fur die Glucose-Bestimmung in Korperflussigkeiten","volume":"13","author":"Von Banauch D.","year":"1975","unstructured":"Von Banauch , D. , W. Brummer , W. Ebeling , H. Metz , H. Rindfrey , and H. Lang . 1975 . Eine Glucose-Dehydrogenase fur die Glucose-Bestimmung in Korperflussigkeiten . Z. Klin. Chem. Klin. Biochem. 13 : 101 - 107 .","journal-title":"Z. Klin. Chem. Klin. Biochem."},{"key":"p_21","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1042\/bj1090811","article-title":"Sporulation in Bacillus subtilis. Biochemical changes","volume":"109","author":"Warren S. C.","year":"1968","unstructured":"Warren , S. C. 1968 . Sporulation in Bacillus subtilis. Biochemical changes . Biochem. J. 109 : 811 - 818 .","journal-title":"Biochem. J."},{"key":"p_22","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1128\/JB.94.3.522-529.1967","article-title":"Separation of two functional roles of L-alanine in the initiation of Bacillus subtilis spore germination","volume":"94","author":"Wax R.","year":"1967","unstructured":"Wax , R. , E. Freese , and M. Cashel . 1967 . Separation of two functional roles of L-alanine in the initiation of Bacillus subtilis spore germination . J. Bacteriol. 94 : 522 - 529 .","journal-title":"J. Bacteriol."}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jb.132.1.282-293.1977","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jb.132.1.282-293.1977","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T17:26:31Z","timestamp":1627579591000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/jb.132.1.282-293.1977"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1977,10]]},"references-count":22,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1977,10]]}},"alternative-id":["10.1128\/jb.132.1.282-293.1977"],"URL":"https:\/\/doi.org\/10.1128\/jb.132.1.282-293.1977","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[1977,10]]},"assertion":[{"value":"2021-02-02","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}