{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,14]],"date-time":"2026-03-14T03:47:17Z","timestamp":1773460037013,"version":"3.50.1"},"reference-count":30,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[1985,4,1]],"date-time":"1985-04-01T00:00:00Z","timestamp":481161600000},"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":[[1985,4]]},"abstract":"<jats:p>The properties of D-1-amino-2-propanol oxidoreductase from wild-type Escherichia coli have been compared with those of a glycerol dehydrogenase from mutant E. coli 424 and of a 1,2-propanediol oxidoreductase from Neisseria gonorrhoeae. Several independent lines of evidence indicate that the former two enzymes are identical. (i) Both enzymatic activities purified to virtual homogeneity in an identical manner, and the ratio of specific activities (glycerol\/aminopropanol) remained constant at all stages. (ii) When electrophoresed, both purified enzymes showed a major as well as a minor band of protein coincident with activity, and these two bands from each enzyme had the same mobility. (iii) The subunit molecular weights and isoelectric points were identical for each enzyme, and (iv) kinetic constants (Km and Vmax values) determined with three different substrates were the same. The somewhat greater stability of the glycerol dehydrogenase to controlled heat denaturation at 74 degrees C was the only difference observed between these two enzymes. In contrast, D-1-amino-2-propanol oxidoreductase was found to be immunochemically and kinetically distinct from the 1,2-propanediol oxidoreductase from N. gonorrhoeae.<\/jats:p>","DOI":"10.1128\/jb.162.1.170-175.1985","type":"journal-article","created":{"date-parts":[[2020,1,3]],"date-time":"2020-01-03T18:06:59Z","timestamp":1578074819000},"page":"170-175","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":17,"title":["Identity of Escherichia coli D-1-amino-2-propanol:NAD+ oxidoreductase with E. coli glycerol dehydrogenase but not with Neisseria gonorrhoeae 1,2-propanediol:NAD+ oxidoreductase"],"prefix":"10.1128","volume":"162","author":[{"given":"J J","family":"Kelley","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E E","family":"Dekker","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"p_2","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/S0006-291X(78)80028-X","article-title":"L-Threonine dehydrogenase of Escherichia coli K-12","volume":"85","author":"Boylan S. A.","year":"1978","unstructured":"Boylan , S. A. , and E. E. Dekker . 1978 . L-Threonine dehydrogenase of Escherichia coli K-12 . Biochem. Biophys. Res. Commun. 85 : 190 - 197 .","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"p_3","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1016\/S0021-9258(19)69880-7","article-title":"L-Threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12","volume":"256","author":"Boylan S. A.","year":"1981","unstructured":"Boylan , S. A. , and E. E. Dekker . 1981 . L-Threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12 . J. Biol. Chem. 256 : 1809 - 1815 .","journal-title":"J. Biol. Chem."},{"key":"p_4","first-page":"432","article-title":"Formation of D-1- amino-2-propanol by enzymes from Escherichia coli K-12. Biochem. Biophys","volume":"53","author":"Campbell R. L.","year":"1973","unstructured":"Campbell , R. L. , and E. E. Dekker . 1973 . Formation of D-1- amino-2-propanol by enzymes from Escherichia coli K-12. Biochem. Biophys , Res. Commun. 53 : 432 - 437 .","journal-title":"Res. Commun."},{"key":"p_5","doi-asserted-by":"crossref","first-page":"7282","DOI":"10.1016\/S0021-9258(17)34497-6","article-title":"Purification, separation, and characterization of two molecular forms of D-1-amino-2-propanol:NAD' oxidoreductase activity from extracts of Escherichia coli K-12","volume":"253","author":"Campbell R. L.","year":"1978","unstructured":"Campbell , R. L. , R. R. Swain , and E. E. Dekker . 1978 . Purification, separation, and characterization of two molecular forms of D-1-amino-2-propanol:NAD' oxidoreductase activity from extracts of Escherichia coli K-12 . J. Biol. Chem. 253 : 7282 - 7288 .","journal-title":"J. Biol. Chem."},{"key":"p_6","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/0304-4165(68)90150-5","article-title":"Formation of D-1-amino-2-propanol by a highly purified enzyme from Escherichia coli","volume":"158","author":"Dekker E. E.","year":"1968","unstructured":"Dekker , E. E. , and R. R. Swain . 1968 . Formation of D-1-amino-2-propanol by a highly purified enzyme from Escherichia coli . Biochim. Biophys. Acta 158 : 306 - 307 .","journal-title":"Biochim. Biophys. Acta"},{"key":"p_7","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/S0021-9258(19)77254-8","article-title":"The amino acid composition of T3 bacteriophage","volume":"205","author":"Fraser D.","year":"1953","unstructured":"Fraser , D. , and E. A. Jerrel . 1953 . The amino acid composition of T3 bacteriophage . J. Biol. Chem. 205 : 291 - 295 .","journal-title":"J. Biol. Chem."},{"key":"p_8","unstructured":"Friedman H. C. 1975. Biosynthesis of corrinoids p. 75-109. In B. B. Baboir (ed.) Cobalamin: biochemistry and pathophysiology. John Wiley & Sons Inc. New York."},{"key":"p_9","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/0076-6879(71)22041-3","article-title":"Analytical gel electrophoresis","volume":"22","author":"Gabriel 0.","year":"1971","unstructured":"Gabriel , 0. 1971 . Analytical gel electrophoresis . Methods Enzymol. 22 : 565 - 578 .","journal-title":"Methods Enzymol."},{"key":"p_10","first-page":"585","article-title":"Locating enzymes on gels","volume":"22","author":"Gabriel 0.","year":"1971","unstructured":"Gabriel , 0. 1971 . Locating enzymes on gels . Methods Enzymol. 22 : 585 - 586 .","journal-title":"Methods Enzymol."},{"key":"p_11","first-page":"407","article-title":"Protein-carbohydrate interaction. III. Agar gel-diffusion studies on the interaction of concanavalin A, a lectin isolated from jack bean, with polysaccharides","volume":"111","author":"Goldstein I. J.","year":"1965","unstructured":"Goldstein , I. J. , and L. L. So. 1965 . Protein-carbohydrate interaction. III. Agar gel-diffusion studies on the interaction of concanavalin A, a lectin isolated from jack bean, with polysaccharides . Arch. Biochem. Biophys. 111 : 407 - 414 .","journal-title":"Arch. Biochem. Biophys."},{"key":"p_12","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/0003-9861(83)90595-7","article-title":"Purification and properties of a NAD-linked 1,2-propanediol dehydrogenase from propane-grown Pseudomonas fluorescens NRRL B-1224","volume":"223","author":"Hou C. T.","year":"1983","unstructured":"Hou , C. T. , R. N. Patel , A , I. Laskin , N. Barnabe , and I. Barist . 1983 . Purification and properties of a NAD-linked 1,2-propanediol dehydrogenase from propane-grown Pseudomonas fluorescens NRRL B-1224 . Arch. Biochem. Biophys. 223 : 297 - 308 .","journal-title":"Arch. Biochem. Biophys."},{"key":"p_13","first-page":"2159","article-title":"Glycerol dehydrogenase production by Geotrichum candidum","volume":"46","author":"Itoh N.","year":"1982","unstructured":"Itoh , N. , and K. Umeda . 1982 . Glycerol dehydrogenase production by Geotrichum candidum . Agric. Biol. Chem. 46 : 2159 - 2161 .","journal-title":"Agric. Biol. Chem."},{"key":"p_14","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1007\/BF02102318","article-title":"Experimental evolution of a novel pathway for glycerol dissimilation in Escherichia coli","volume":"19","author":"Jin R. Z.","year":"1983","unstructured":"Jin , R. Z. , J. C. -T. Tang , and E. C. C. Lin . 1983 . Experimental evolution of a novel pathway for glycerol dissimilation in Escherichia coli . J. Mol. Evol. 19 : 429 - 436 .","journal-title":"J. Mol. Evol."},{"key":"p_15","doi-asserted-by":"crossref","unstructured":"Kelley J. J. and E. E. Dekker. 1984. D-1-Amino-2- propanol:NAD+ oxidoreductase. Purification and general properties of the large molecular form of the enzyme from Escherichia coli K-12. J. Biol. Chem. 259;2124-2129.","DOI":"10.1016\/S0021-9258(17)43325-4"},{"key":"p_16","doi-asserted-by":"crossref","first-page":"1820","DOI":"10.1016\/S0021-9258(19)76888-4","article-title":"The activation of glycerol dehydrogenase from Aerobacter aerogenes by monovalent cations","volume":"235","author":"Lin E. C. C.","year":"1960","unstructured":"Lin , E. C. C. , and B. Magasanik . 1960 . The activation of glycerol dehydrogenase from Aerobacter aerogenes by monovalent cations . J. Biol. Chem. 235 : 1820 - 1823 .","journal-title":"J. Biol. Chem."},{"key":"p_17","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1099\/00221287-63-1-49","article-title":"Microbial metabolism of aminoketones. D-1-aminopropan-2-ol and aminoacetone metabolism in Escherichia coli","volume":"63","author":"Lowe D. A.","year":"1970","unstructured":"Lowe , D. A. , and J. M. Turner . 1970 . Microbial metabolism of aminoketones. D-1-aminopropan-2-ol and aminoacetone metabolism in Escherichia coli . J. Gen. Microbiol. 63 : 49 - 61 .","journal-title":"J. Gen. Microbiol."},{"key":"p_18","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_19","first-page":"451","article-title":"The isolation and characterization of a 1,2-propanediol oxidoreductase from Neisseria gonorrhoeae","volume":"119","author":"McDonald H. C.","year":"1980","unstructured":"McDonald , H. C. , M. M. Takagushi , C. C. Detar , P. A. Simon , K. A. Livsey , G. Odstrechel , N. 0. Kaplan , and H. H. Weetall . 1980 . The isolation and characterization of a 1,2-propanediol oxidoreductase from Neisseria gonorrhoeae . J. Gen. Microbiol. 119 : 451 - 458 .","journal-title":"J. Gen. Microbiol."},{"key":"p_20","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/0006-3002(60)90388-7","article-title":"The enzymic conversion of threonine to aminoacetone","volume":"41","author":"Neuberger A.","year":"1960","unstructured":"Neuberger , A. , and G. H. Tait . 1960 . The enzymic conversion of threonine to aminoacetone . Biochim. Biophys. Acta 41 : 164 - 165 .","journal-title":"Biochim. Biophys. Acta"},{"key":"p_21","doi-asserted-by":"crossref","first-page":"4007","DOI":"10.1016\/S0021-9258(19)41496-8","article-title":"High resolution two-dimensional electrophoresis of proteins","volume":"250","author":"O'Farrell P. H.","year":"1975","unstructured":"O'Farrell , P. H. 1975 . High resolution two-dimensional electrophoresis of proteins . J. Biol. Chem. 250 : 4007 - 4021 .","journal-title":"J. Biol. Chem."},{"key":"p_22","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1093\/oxfordjournals.jbchem.a133678","article-title":"Specific affinity of glycerol dehydrogenase from Geotrichium candidium for 10- carboxydecyl-Sepharose: its application for the purification of the enyzme","volume":"91","author":"Sasaki E.","year":"1982","unstructured":"Sasaki , E. , N. Itoh , H. Goto , R. Yamamoto , H. Tanaka , K. Yamashita , J. Yamashita , and T. Horio . 1982 . Specific affinity of glycerol dehydrogenase from Geotrichium candidium for 10- carboxydecyl-Sepharose: its application for the purification of the enyzme . J. Biochem. 91 : 211 - 217 .","journal-title":"J. Biochem."},{"key":"p_23","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1515\/bchm2.1983.364.2.911","article-title":"Isolation and characterization of glycerol dehydrogenase from Bacillus megaterium","volume":"364","author":"Scharschmidt M.","year":"1983","unstructured":"Scharschmidt , M. , G. Pfleiderer , H. Metz , and W. Brummer . 1983 . Isolation and characterization of glycerol dehydrogenase from Bacillus megaterium . Hoppe-Seyler's Z. Physiol. Chem. 364 : 911 - 921 .","journal-title":"Hoppe-Seyler's Z. Physiol. Chem."},{"key":"p_24","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1128\/jb.152.3.1169-1174.1982","article-title":"Immunochemical properties of NAD+-linked glycerol dehydrogenases from Escherichia coli and Klebsiella pneumoniae","volume":"152","author":"Tang J. C.","year":"1982","unstructured":"Tang , J. C. - T. , R. G. Forage , and E. C. C. Lin . 1982 . Immunochemical properties of NAD+-linked glycerol dehydrogenases from Escherichia coli and Klebsiella pneumoniae . J. Bacteriol. 152 : 1169 - 1174 .","journal-title":"J. Bacteriol."},{"key":"p_25","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1128\/JB.140.1.182-187.1979","article-title":"Purification and properties of a nicotinamide adenine dinucleotide-linked dehydrogenase that serves an Escherichia coli mutant for glycerol catabolism","volume":"140","author":"Tang J. C.","year":"1979","unstructured":"Tang , J. C. - T. , F. E. Ruch , Jr. , and E. C. C. Lin . 1979 . Purification and properties of a nicotinamide adenine dinucleotide-linked dehydrogenase that serves an Escherichia coli mutant for glycerol catabolism . J. Bacteriol. 140 : 182 - 187 .","journal-title":"J. Bacteriol."},{"key":"p_26","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1128\/jb.152.3.1001-1007.1982","article-title":"Derepression of an NAD-linked dehydro$enase that serves an Escherichia coli mutant for growth on glycerol","volume":"152","author":"Tang J. C.","year":"1982","unstructured":"Tang , J. C. - T. , E. J. St. Martin , and E. C. C. Lin . 1982 . Derepression of an NAD-linked dehydro$enase that serves an Escherichia coli mutant for growth on glycerol . J. Bacteriol. 152 : 1001 - 1007 .","journal-title":"J. Bacteriol."},{"key":"p_27","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1016\/0006-3002(60)90197-9","article-title":"Stereoisomeric specificities of 2,3-butanediol dehydrogenases","volume":"39","author":"Taylor M. B.","year":"1960","unstructured":"Taylor , M. B. , and E. Juni . 1960 . Stereoisomeric specificities of 2,3-butanediol dehydrogenases . Biochim. Biophys. Acta. 39 : 448 - 457 .","journal-title":"Biochim. Biophys. Acta."},{"key":"p_28","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1042\/bj0990427","article-title":"Microbial metabolism of aminoketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrogenase in Escherichia coli","volume":"99","author":"Turner J. M.","year":"1966","unstructured":"Turner , J. M. 1966 . Microbial metabolism of aminoketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrogenase in Escherichia coli . Biochem. J. 99 : 427 - 433 .","journal-title":"Biochem. J."},{"key":"p_29","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0076-6879(72)26003-7","article-title":"Measurement of molecular weights by electrophoresis on SDS-acrylamide gel","volume":"26","author":"Weber K.","year":"1972","unstructured":"Weber , K. , J. R. Pringle , and M. Osborn . 1972 . Measurement of molecular weights by electrophoresis on SDS-acrylamide gel . Methods Enzymol. 26 : 3 - 27 .","journal-title":"Methods Enzymol."},{"key":"p_30","first-page":"2325","article-title":"Formation of glycerol dehydrogenase by microorganisms","volume":"46","author":"Yamada H.","year":"1982","unstructured":"Yamada , H. , A. Nagao , H. Nishise , and Y. Tani . 1982 . Formation of glycerol dehydrogenase by microorganisms . Agric. Biol. Chem. 46 : 2325 - 2332 .","journal-title":"Agric. Biol. Chem."},{"key":"p_31","first-page":"2333","article-title":"Glycerol dehydrogenase from Cellulomonas sp. NT3060: purification and characterization","volume":"46","author":"Yamada H.","year":"1982","unstructured":"Yamada , H. , A. Nagao , H. Nishise , and Y. Tani . 1982 . Glycerol dehydrogenase from Cellulomonas sp. NT3060: purification and characterization . Agric. Biol. Chem. 46 : 2333 - 2339 .","journal-title":"Agric. Biol. Chem."}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jb.162.1.170-175.1985","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jb.162.1.170-175.1985","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,10,9]],"date-time":"2022-10-09T22:25:52Z","timestamp":1665354352000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/jb.162.1.170-175.1985"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1985,4]]},"references-count":30,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1985,4]]}},"alternative-id":["10.1128\/jb.162.1.170-175.1985"],"URL":"https:\/\/doi.org\/10.1128\/jb.162.1.170-175.1985","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[1985,4]]},"assertion":[{"value":"2021-02-02","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}