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sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus.
Staphylococcus aureus has membrane-associated sn-glycerol-3-phosphate dehydrogenase activity that is strongly activated by detergents. The enzyme can be measured spectrophotometrically in intact cells in assay systems containing lauryldimethylamine oxide (Ammonyx LO). The dehydrogenase activity was...
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pubmed-2220672003-12-01 sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus. Lascelles, J J Bacteriol Research Article Staphylococcus aureus has membrane-associated sn-glycerol-3-phosphate dehydrogenase activity that is strongly activated by detergents. The enzyme can be measured spectrophotometrically in intact cells in assay systems containing lauryldimethylamine oxide (Ammonyx LO). The dehydrogenase activity was located exclusively in the membrane fraction of cells grown with glycerol under aerobic conditions or under anaerobic conditions with the addition of nitrate; there was no evidence of multiple forms. Development of sn-glycerol-3-phosphate dehydrogenase activity was studied with suspensions of cells grown previously under semianaerobic conditions with glucose and nitrate. The wild-type strain rapidly formed the enzyme when incubated with glycerol under aerobic conditions or under semianaerobic conditions in the presence of nitrate. Under similar conditions, suspensions of hem mutant H-14 required the addition of hemin. Induction of the enzyme was strongly repressed by glucose with both organisms. A procedure was established to obtain cells of mutant H-14 with sn-glycerol-3-phosphate dehydrogenase and nitrate reductase activities, but which could not link the systems unless supplemented with hemin. The coupled activity could also be reconstructed in vitro by the addition of hemin to the depleted membranes. 1978-02 /pmc/articles/PMC222067/ /pubmed/637913 Text en |
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US National Library of Medicine |
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PubMed Central |
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Research Article Research Article Research Article Enzymology Genetics and Molecular Biology Research Article Research Article Genetics and Molecular Biology Research Article Research Article Research Article Research Article Physiology and Metabolism Physiology and Metabolism Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Physiology and Metabolism Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Physiology and Metabolism Research Article Research Article Research Article Research Article Research Article Research Article Research Article Physiology and Metabolism Research Article Morphology and Ultrastructure Research Article Research Article Research Article Research Article Genetics and Molecular Biology Research Article Research Article |
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Research Article Research Article Research Article Enzymology Genetics and Molecular Biology Research Article Research Article Genetics and Molecular Biology Research Article Research Article Research Article Research Article Physiology and Metabolism Physiology and Metabolism Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Physiology and Metabolism Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Research Article Physiology and Metabolism Research Article Research Article Research Article Research Article Research Article Research Article Research Article Physiology and Metabolism Research Article Morphology and Ultrastructure Research Article Research Article Research Article Research Article Genetics and Molecular Biology Research Article Research Article Lascelles, J DeMoss, J A Cornett, J B Redman, B E Shockman, G D Patel, Ramesh N. Hou, Ching T. Felix, Andre Simonian, Michael H. Goldstein, Ruth V. Mosteller, Raymond D. Wookey, P Rosenberg, H Lindgren, V Dantzig, Anne H. Zurowski, Wayne K. Ball, Thomas M. Nason, Alvin Friedrich, B Magasanik, B Friedrich, B Friedrich, C G Magasanik, B Woodward, J R Cirillo, V P Edmunds, L N Ubelaker, M H Rosenblum, E D Melton, Thoyd Hartman, Philip E. Stratis, John P. Lee, Timothy L. Davis, Alan T. Phibbs, P. V. McCowen, S. M. Feary, T. W. Blevins, W. T. Perlman, D Ratzkin, B Grabnar, M Roth, J Ratzkin, B Roth, J Kung, F C Glaser, D A Bretscher, A P Kaiser, D Hartman, P S Eisenstark, A Foster, J W Moat, A G Mazón, M J Dolin, M. I. Juni, E. Reichenbecher, V E Fischer, M Gross, S R Reichenbecher, V E Gross, S R Lee, W L Shalita, A R Poh-Fitzpatrick, M B Chi, N Y Ehrlich, S D Lederberg, J Hinks, R P Daneo-Moore, L Shockman, G D Winkler, M E Roth, D J Hartman, P E Gottesman, S Zipser, D Stuart, J G Ferretti, J J Webb, R B Hemmings, Brian A. Materman, E C Van Gool, A P Pannekoek, H Noordermeer, I A van Sluis, C A van de Putte, P Bernhard, K Schrempf, H Goebel, W Suzuki, T Iino, T Horiguchi, T Yamaguchi, S Oka, A Patel, K R Mayberry-Carson, K J Smith, P F Chester, I R Murray, R G Lin, T. S. Kolattukudy, P. E. Käppeli, O Müller, M Fiechter, A Burdett, I. D. J. Higgins, M. L. Baron, E S Saz, A K Agabian, N Unger, B Long, W S Slayman, C L Low, K B Tomchika, K I Hong, J S Lee, Suzanne Y. Bailey, Stephen C. Apirion, David Johnstone, K Ellar, D J Parag, Y sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus. |
| description |
Staphylococcus aureus has membrane-associated sn-glycerol-3-phosphate dehydrogenase activity that is strongly activated by detergents. The enzyme can be measured spectrophotometrically in intact cells in assay systems containing lauryldimethylamine oxide (Ammonyx LO). The dehydrogenase activity was located exclusively in the membrane fraction of cells grown with glycerol under aerobic conditions or under anaerobic conditions with the addition of nitrate; there was no evidence of multiple forms. Development of sn-glycerol-3-phosphate dehydrogenase activity was studied with suspensions of cells grown previously under semianaerobic conditions with glucose and nitrate. The wild-type strain rapidly formed the enzyme when incubated with glycerol under aerobic conditions or under semianaerobic conditions in the presence of nitrate. Under similar conditions, suspensions of hem mutant H-14 required the addition of hemin. Induction of the enzyme was strongly repressed by glucose with both organisms. A procedure was established to obtain cells of mutant H-14 with sn-glycerol-3-phosphate dehydrogenase and nitrate reductase activities, but which could not link the systems unless supplemented with hemin. The coupled activity could also be reconstructed in vitro by the addition of hemin to the depleted membranes. |
| author |
Lascelles, J DeMoss, J A Cornett, J B Redman, B E Shockman, G D Patel, Ramesh N. Hou, Ching T. Felix, Andre Simonian, Michael H. Goldstein, Ruth V. Mosteller, Raymond D. Wookey, P Rosenberg, H Lindgren, V Dantzig, Anne H. Zurowski, Wayne K. Ball, Thomas M. Nason, Alvin Friedrich, B Magasanik, B Friedrich, B Friedrich, C G Magasanik, B Woodward, J R Cirillo, V P Edmunds, L N Ubelaker, M H Rosenblum, E D Melton, Thoyd Hartman, Philip E. Stratis, John P. Lee, Timothy L. Davis, Alan T. Phibbs, P. V. McCowen, S. M. Feary, T. W. Blevins, W. T. Perlman, D Ratzkin, B Grabnar, M Roth, J Ratzkin, B Roth, J Kung, F C Glaser, D A Bretscher, A P Kaiser, D Hartman, P S Eisenstark, A Foster, J W Moat, A G Mazón, M J Dolin, M. I. Juni, E. Reichenbecher, V E Fischer, M Gross, S R Reichenbecher, V E Gross, S R Lee, W L Shalita, A R Poh-Fitzpatrick, M B Chi, N Y Ehrlich, S D Lederberg, J Hinks, R P Daneo-Moore, L Shockman, G D Winkler, M E Roth, D J Hartman, P E Gottesman, S Zipser, D Stuart, J G Ferretti, J J Webb, R B Hemmings, Brian A. Materman, E C Van Gool, A P Pannekoek, H Noordermeer, I A van Sluis, C A van de Putte, P Bernhard, K Schrempf, H Goebel, W Suzuki, T Iino, T Horiguchi, T Yamaguchi, S Oka, A Patel, K R Mayberry-Carson, K J Smith, P F Chester, I R Murray, R G Lin, T. S. Kolattukudy, P. E. Käppeli, O Müller, M Fiechter, A Burdett, I. D. J. Higgins, M. L. Baron, E S Saz, A K Agabian, N Unger, B Long, W S Slayman, C L Low, K B Tomchika, K I Hong, J S Lee, Suzanne Y. Bailey, Stephen C. Apirion, David Johnstone, K Ellar, D J Parag, Y |
| author_facet |
Lascelles, J DeMoss, J A Cornett, J B Redman, B E Shockman, G D Patel, Ramesh N. Hou, Ching T. Felix, Andre Simonian, Michael H. Goldstein, Ruth V. Mosteller, Raymond D. Wookey, P Rosenberg, H Lindgren, V Dantzig, Anne H. Zurowski, Wayne K. Ball, Thomas M. Nason, Alvin Friedrich, B Magasanik, B Friedrich, B Friedrich, C G Magasanik, B Woodward, J R Cirillo, V P Edmunds, L N Ubelaker, M H Rosenblum, E D Melton, Thoyd Hartman, Philip E. Stratis, John P. Lee, Timothy L. Davis, Alan T. Phibbs, P. V. McCowen, S. M. Feary, T. W. Blevins, W. T. Perlman, D Ratzkin, B Grabnar, M Roth, J Ratzkin, B Roth, J Kung, F C Glaser, D A Bretscher, A P Kaiser, D Hartman, P S Eisenstark, A Foster, J W Moat, A G Mazón, M J Dolin, M. I. Juni, E. Reichenbecher, V E Fischer, M Gross, S R Reichenbecher, V E Gross, S R Lee, W L Shalita, A R Poh-Fitzpatrick, M B Chi, N Y Ehrlich, S D Lederberg, J Hinks, R P Daneo-Moore, L Shockman, G D Winkler, M E Roth, D J Hartman, P E Gottesman, S Zipser, D Stuart, J G Ferretti, J J Webb, R B Hemmings, Brian A. Materman, E C Van Gool, A P Pannekoek, H Noordermeer, I A van Sluis, C A van de Putte, P Bernhard, K Schrempf, H Goebel, W Suzuki, T Iino, T Horiguchi, T Yamaguchi, S Oka, A Patel, K R Mayberry-Carson, K J Smith, P F Chester, I R Murray, R G Lin, T. S. Kolattukudy, P. E. Käppeli, O Müller, M Fiechter, A Burdett, I. D. J. Higgins, M. L. Baron, E S Saz, A K Agabian, N Unger, B Long, W S Slayman, C L Low, K B Tomchika, K I Hong, J S Lee, Suzanne Y. Bailey, Stephen C. Apirion, David Johnstone, K Ellar, D J Parag, Y |
| author_sort |
Lascelles, J |
| title |
sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus. |
| title_short |
sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus. |
| title_full |
sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus. |
| title_fullStr |
sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus. |
| title_full_unstemmed |
sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus. |
| title_sort |
sn-glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of staphylococcus aureus. |
| publishDate |
1978 |
| url |
https://ncbi.nlm.nih.gov/pmc/articles/PMC222067/ https://ncbi.nlm.nih.gov/pubmed/637913 https://ncbi.nlm.nih.gov/pmc/articles/PMC222068/ https://ncbi.nlm.nih.gov/pubmed/342499 https://ncbi.nlm.nih.gov/pmc/articles/PMC222069/ https://ncbi.nlm.nih.gov/pubmed/415045 https://ncbi.nlm.nih.gov/pmc/articles/PMC222070/ https://ncbi.nlm.nih.gov/pubmed/415046 https://ncbi.nlm.nih.gov/pmc/articles/PMC222071/ https://ncbi.nlm.nih.gov/pubmed/342500 https://ncbi.nlm.nih.gov/pmc/articles/PMC222072/ https://ncbi.nlm.nih.gov/pubmed/146699 https://ncbi.nlm.nih.gov/pmc/articles/PMC222073/ https://ncbi.nlm.nih.gov/pubmed/415047 https://ncbi.nlm.nih.gov/pmc/articles/PMC222074/ https://ncbi.nlm.nih.gov/pubmed/146700 https://ncbi.nlm.nih.gov/pmc/articles/PMC222075/ https://ncbi.nlm.nih.gov/pubmed/342501 https://ncbi.nlm.nih.gov/pmc/articles/PMC222076/ https://ncbi.nlm.nih.gov/pubmed/24039 https://ncbi.nlm.nih.gov/pmc/articles/PMC222077/ https://ncbi.nlm.nih.gov/pubmed/342502 https://ncbi.nlm.nih.gov/pmc/articles/PMC222078/ https://ncbi.nlm.nih.gov/pubmed/342503 https://ncbi.nlm.nih.gov/pmc/articles/PMC222079/ https://ncbi.nlm.nih.gov/pubmed/342504 https://ncbi.nlm.nih.gov/pmc/articles/PMC222080/ https://ncbi.nlm.nih.gov/pubmed/146701 https://ncbi.nlm.nih.gov/pmc/articles/PMC222081/ https://ncbi.nlm.nih.gov/pubmed/342505 https://ncbi.nlm.nih.gov/pmc/articles/PMC222082/ https://ncbi.nlm.nih.gov/pubmed/342506 https://ncbi.nlm.nih.gov/pmc/articles/PMC222083/ https://ncbi.nlm.nih.gov/pubmed/342507 https://ncbi.nlm.nih.gov/pmc/articles/PMC222084/ https://ncbi.nlm.nih.gov/pubmed/627535 https://ncbi.nlm.nih.gov/pmc/articles/PMC222085/ https://ncbi.nlm.nih.gov/pubmed/415048 https://ncbi.nlm.nih.gov/pmc/articles/PMC222086/ https://ncbi.nlm.nih.gov/pubmed/342508 https://ncbi.nlm.nih.gov/pmc/articles/PMC222087/ https://ncbi.nlm.nih.gov/pubmed/203571 https://ncbi.nlm.nih.gov/pmc/articles/PMC222088/ https://ncbi.nlm.nih.gov/pubmed/24040 https://ncbi.nlm.nih.gov/pmc/articles/PMC222089/ https://ncbi.nlm.nih.gov/pubmed/627536 https://ncbi.nlm.nih.gov/pmc/articles/PMC222090/ https://ncbi.nlm.nih.gov/pubmed/146702 https://ncbi.nlm.nih.gov/pmc/articles/PMC222091/ https://ncbi.nlm.nih.gov/pubmed/146703 https://ncbi.nlm.nih.gov/pmc/articles/PMC222092/ https://ncbi.nlm.nih.gov/pubmed/637914 https://ncbi.nlm.nih.gov/pmc/articles/PMC222093/ https://ncbi.nlm.nih.gov/pubmed/415049 https://ncbi.nlm.nih.gov/pmc/articles/PMC222094/ https://ncbi.nlm.nih.gov/pubmed/415050 https://ncbi.nlm.nih.gov/pmc/articles/PMC222095/ https://ncbi.nlm.nih.gov/pubmed/342509 https://ncbi.nlm.nih.gov/pmc/articles/PMC222096/ https://ncbi.nlm.nih.gov/pubmed/146704 https://ncbi.nlm.nih.gov/pmc/articles/PMC222097/ https://ncbi.nlm.nih.gov/pubmed/342510 https://ncbi.nlm.nih.gov/pmc/articles/PMC222098/ https://ncbi.nlm.nih.gov/pubmed/342511 https://ncbi.nlm.nih.gov/pmc/articles/PMC222099/ https://ncbi.nlm.nih.gov/pubmed/24041 https://ncbi.nlm.nih.gov/pmc/articles/PMC222100/ https://ncbi.nlm.nih.gov/pubmed/342512 https://ncbi.nlm.nih.gov/pmc/articles/PMC222101/ https://ncbi.nlm.nih.gov/pubmed/342513 https://ncbi.nlm.nih.gov/pmc/articles/PMC222102/ https://ncbi.nlm.nih.gov/pubmed/415051 https://ncbi.nlm.nih.gov/pmc/articles/PMC222103/ https://ncbi.nlm.nih.gov/pubmed/342514 https://ncbi.nlm.nih.gov/pmc/articles/PMC222104/ https://ncbi.nlm.nih.gov/pubmed/342515 https://ncbi.nlm.nih.gov/pmc/articles/PMC222105/ https://ncbi.nlm.nih.gov/pubmed/24042 https://ncbi.nlm.nih.gov/pmc/articles/PMC222106/ https://ncbi.nlm.nih.gov/pubmed/627537 https://ncbi.nlm.nih.gov/pmc/articles/PMC222107/ https://ncbi.nlm.nih.gov/pubmed/415052 https://ncbi.nlm.nih.gov/pmc/articles/PMC222108/ https://ncbi.nlm.nih.gov/pubmed/627538 https://ncbi.nlm.nih.gov/pmc/articles/PMC222109/ https://ncbi.nlm.nih.gov/pubmed/415053 https://ncbi.nlm.nih.gov/pmc/articles/PMC222110/ https://ncbi.nlm.nih.gov/pubmed/415054 https://ncbi.nlm.nih.gov/pmc/articles/PMC222111/ https://ncbi.nlm.nih.gov/pubmed/627539 https://ncbi.nlm.nih.gov/pmc/articles/PMC222112/ https://ncbi.nlm.nih.gov/pubmed/342516 https://ncbi.nlm.nih.gov/pmc/articles/PMC222113/ https://ncbi.nlm.nih.gov/pubmed/342485 https://ncbi.nlm.nih.gov/pmc/articles/PMC222114/ https://ncbi.nlm.nih.gov/pubmed/342486 https://ncbi.nlm.nih.gov/pmc/articles/PMC222115/ https://ncbi.nlm.nih.gov/pubmed/415036 https://ncbi.nlm.nih.gov/pmc/articles/PMC222116/ https://ncbi.nlm.nih.gov/pubmed/415037 |
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