Статті в журналах з теми "Methylmalonyl coenzyme A mutase"
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Vrijbloed, Jan W., Katja Zerbe-Burkhardt, Ananda Ratnatilleke, Andreas Grubelnik-Leiser, and John A. Robinson. "Insertional Inactivation of Methylmalonyl Coenzyme A (CoA) Mutase and Isobutyryl-CoA Mutase Genes in Streptomyces cinnamonensis: Influence on Polyketide Antibiotic Biosynthesis." Journal of Bacteriology 181, no. 18 (September 15, 1999): 5600–5605. http://dx.doi.org/10.1128/jb.181.18.5600-5605.1999.
Повний текст джерелаBotella, Laure, Nic D. Lindley, and Lothar Eggeling. "Formation and Metabolism of Methylmalonyl Coenzyme A in Corynebacterium glutamicum." Journal of Bacteriology 191, no. 8 (February 20, 2009): 2899–901. http://dx.doi.org/10.1128/jb.01756-08.
Повний текст джерелаZhang, Weiwen, and Kevin A. Reynolds. "MeaA, a Putative Coenzyme B12-Dependent Mutase, Provides Methylmalonyl Coenzyme A for Monensin Biosynthesis in Streptomyces cinnamonensis." Journal of Bacteriology 183, no. 6 (March 15, 2001): 2071–80. http://dx.doi.org/10.1128/jb.183.6.2071-2080.2001.
Повний текст джерелаCarlucci, Filippo, Francesca Rosi, Valentina Tommassini, and Antonella Tabucchi. "CE assay of methylmalonyl-coenzyme-A mutase activity." ELECTROPHORESIS 28, no. 12 (June 2007): 1921–25. http://dx.doi.org/10.1002/elps.200700031.
Повний текст джерелаZhao, Yimin, Martina Michenfelder, and János Rétey. "Synthesis, characterization, and enzymic conversion of nonhydrolysable analogues of propionylcoenzyme A." Canadian Journal of Chemistry 72, no. 1 (January 1, 1994): 164–69. http://dx.doi.org/10.1139/v94-025.
Повний текст джерелаBanerjee, R., and M. Vlasie. "Controlling the reactivity of radical intermediates by coenzyme B12-dependent methylmalonyl-CoA mutase." Biochemical Society Transactions 30, no. 4 (August 1, 2002): 621–24. http://dx.doi.org/10.1042/bst0300621.
Повний текст джерелаWatanabe, Fumio, Yoshiyuki Tamura, Hisako Saido, and Yoshihisa Nakano. "Enzymatic Assay for Adenosylcobalamin-dependent Methylmalonyl Coenzyme A Mutase." Bioscience, Biotechnology, and Biochemistry 57, no. 9 (January 1993): 1593–94. http://dx.doi.org/10.1271/bbb.57.1593.
Повний текст джерелаKeep, N. H., G. A. Smith, M. C. W. Evans, G. P. Diakun, and P. F. Leadlay. "The synthetic substrate succinyl(carbadethia)-CoA generates cob(II)alamin on adenosylcobalamin-dependent methylmalonyl-CoA mutase." Biochemical Journal 295, no. 2 (October 15, 1993): 387–92. http://dx.doi.org/10.1042/bj2950387.
Повний текст джерелаRiedel, B., P. M. Ueland, and A. M. Svardal. "Fully automated assay for cobalamin-dependent methylmalonyl CoA mutase." Clinical Chemistry 41, no. 8 (August 1, 1995): 1164–70. http://dx.doi.org/10.1093/clinchem/41.8.1164.
Повний текст джерелаBito, Tomohiro, Mariko Bito, Tomomi Hirooka, Naho Okamoto, Naoki Harada, Ryoichi Yamaji, Yoshihisa Nakano, Hiroshi Inui, and Fumio Watanabe. "Biological Activity of Pseudovitamin B12 on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells." Molecules 25, no. 14 (July 17, 2020): 3268. http://dx.doi.org/10.3390/molecules25143268.
Повний текст джерелаSharar, Sam R., Charles M. Haberkern, Rhona Jack, and C. Ronald Scott. "Anesthetic Management of a Child With Methylmalonyl-Coenzyme A Mutase Deficiency." Anesthesia & Analgesia 73, no. 4 (October 1991): 499???501. http://dx.doi.org/10.1213/00000539-199110000-00025.
Повний текст джерелаDhansura, Tasneem, Nabila Shaikh, MukhtadirGulam Hashmi, and Chandrakant Shah. "Anaesthetic considerations in a patient with methylmalonyl-coenzyme A mutase deficiency." Indian Journal of Anaesthesia 61, no. 12 (2017): 1018. http://dx.doi.org/10.4103/ija.ija_463_17.
Повний текст джерелаDai, Siyu, Yanting Yang, Yaqian Li, and Hongqian Liu. "Impaired Function of a Rare Mutation in the MMUT Gene Causes Methylmalonic Acidemia in a Chinese Patient." Genetics Research 2022 (July 22, 2022): 1–6. http://dx.doi.org/10.1155/2022/5611697.
Повний текст джерелаHan, Yejun, Aaron S. Hawkins, Michael W. W. Adams, and Robert M. Kelly. "Epimerase (Msed_0639) and Mutase (Msed_0638 and Msed_2055) Convert (S)-Methylmalonyl-Coenzyme A (CoA) to Succinyl-CoA in the Metallosphaera sedula 3-Hydroxypropionate/4-Hydroxybutyrate Cycle." Applied and Environmental Microbiology 78, no. 17 (June 29, 2012): 6194–202. http://dx.doi.org/10.1128/aem.01312-12.
Повний текст джерелаWeichler, Maria-Teresa, Nadya Kurteva-Yaneva, Denise Przybylski, Judith Schuster, Roland H. Müller, Hauke Harms, and Thore Rohwerder. "Thermophilic Coenzyme B12-Dependent Acyl Coenzyme A (CoA) Mutase from Kyrpidia tusciae DSM 2912 Preferentially Catalyzes Isomerization of (R)-3-Hydroxybutyryl-CoA and 2-Hydroxyisobutyryl-CoA." Applied and Environmental Microbiology 81, no. 14 (April 24, 2015): 4564–72. http://dx.doi.org/10.1128/aem.00716-15.
Повний текст джерелаEvans, P. R., and F. Mancia. "How coenzyme B12radicals are generated: methylmalonyl-CoA mutase at 2 Å resolution." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C69. http://dx.doi.org/10.1107/s0108767396096316.
Повний текст джерелаCrane, A. M., R. Jansen, E. R. Andrews, and F. D. Ledley. "Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria." Journal of Clinical Investigation 89, no. 2 (February 1, 1992): 385–91. http://dx.doi.org/10.1172/jci115597.
Повний текст джерелаAldor, Ilana S., Seon-Won Kim, Kristala L. Jones Prather, and Jay D. Keasling. "Metabolic Engineering of a Novel Propionate-Independent Pathway for the Production of Poly(3-Hydroxybutyrate-co-3-Hydroxyvalerate) in Recombinant Salmonella enterica Serovar Typhimurium." Applied and Environmental Microbiology 68, no. 8 (August 2002): 3848–54. http://dx.doi.org/10.1128/aem.68.8.3848-3854.2002.
Повний текст джерелаGonzález-Montaña, Jose-Ramiro, Francisco Escalera-Valente, Angel J. Alonso, Juan M. Lomillos, Roberto Robles, and Marta E. Alonso. "Relationship between Vitamin B12 and Cobalt Metabolism in Domestic Ruminant: An Update." Animals 10, no. 10 (October 12, 2020): 1855. http://dx.doi.org/10.3390/ani10101855.
Повний текст джерелаBermúdez, Omaira, Patricia Padilla, Carlos Huitrón, and MarıÄa Elena Flores. "Influence of carbon and nitrogen source on synthesis of NADP+-isocitrate dehydrogenase, methylmalonyl-coenzyme A mutase, and methylmalonyl-coenzyme A decarboxylase inSaccharopolyspora erythraeaCA340." FEMS Microbiology Letters 164, no. 1 (July 1998): 77–82. http://dx.doi.org/10.1111/j.1574-6968.1998.tb13070.x.
Повний текст джерелаSun, Fangping, and Tamis Darbre. "The Co(i) induced methylmalonyl-succinyl rearrangement in a model for the coenzyme B12 dependent methylmalonyl-CoA mutase." Organic & Biomolecular Chemistry 1, no. 18 (2003): 3154. http://dx.doi.org/10.1039/b305782h.
Повний текст джерелаVALENCE, FLORENCE, ROMAIN RICHOUX, ANNE THIERRY, AIRI PALVA, and SYLVIE LORTAL. "Autolysis of Lactobacillus helveticus and Propionibacterium freudenreichii in Swiss cheeses: first evidence by using species-specific lysis markers." Journal of Dairy Research 65, no. 4 (November 1998): 609–20. http://dx.doi.org/10.1017/s0022029998003021.
Повний текст джерелаRuetz, Markus, Gregory C. Campanello, Meredith Purchal, Hongying Shen, Liam McDevitt, Harsha Gouda, Shoko Wakabayashi, et al. "Itaconyl-CoA forms a stable biradical in methylmalonyl-CoA mutase and derails its activity and repair." Science 366, no. 6465 (October 31, 2019): 589–93. http://dx.doi.org/10.1126/science.aay0934.
Повний текст джерелаPadmakumar, Rugmini, Shinichi Taoka, Raghavaikamal Padmakumar, and Ruma Banerjee. "Coenzyme B12 Is Coordinated by Histidine and Not Dimethylbenzimidazole on Methylmalonyl-CoA Mutase." Journal of the American Chemical Society 117, no. 26 (July 1995): 7033–34. http://dx.doi.org/10.1021/ja00131a039.
Повний текст джерелаPaizs, Csaba, Tanja Diemer, and János Rétey. "The putative coenzyme B12-dependent methylmalonyl-CoA mutase from potatoes is a phosphatase." Bioorganic Chemistry 36, no. 6 (December 2008): 261–64. http://dx.doi.org/10.1016/j.bioorg.2008.06.002.
Повний текст джерелаBermúdez, O. "Influence of carbon and nitrogen source on synthesis of NADP+-isocitrate dehydrogenase, methylmalonyl-coenzyme A mutase, and methylmalonyl-coenzyme A decarboxylase in Saccharopolyspora erythraea CA340." FEMS Microbiology Letters 164, no. 1 (July 1, 1998): 77–82. http://dx.doi.org/10.1016/s0378-1097(98)00198-0.
Повний текст джерелаMancia, Filippo, Nicholas H. Keep, Atsushi Nakagawa, Peter F. Leadlay, Sean McSweeney, Bjarne Rasmussen, Peter Bö secke, Olivier Diat, and Philip R. Evans. "How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 å resolution." Structure 4, no. 3 (March 1996): 339–50. http://dx.doi.org/10.1016/s0969-2126(96)00037-8.
Повний текст джерелаSavvi, Suzana, Digby F. Warner, Bavesh D. Kana, John D. McKinney, Valerie Mizrahi, and Stephanie S. Dawes. "Functional Characterization of a Vitamin B12-Dependent Methylmalonyl Pathway in Mycobacterium tuberculosis: Implications for Propionate Metabolism during Growth on Fatty Acids." Journal of Bacteriology 190, no. 11 (March 28, 2008): 3886–95. http://dx.doi.org/10.1128/jb.01767-07.
Повний текст джерелаScheuring, Eva, Rugmini Padmakumar, Ruma Banerjee, and Mark R. Chance. "Extended X-ray Absorption Fine Structure Analysis of Coenzyme B12Bound to Methylmalonyl-Coenzyme A Mutase Using Global Mapping Techniques†." Journal of the American Chemical Society 119, no. 50 (December 1997): 12192–200. http://dx.doi.org/10.1021/ja9635239.
Повний текст джерелаVlasie, Monica, Shantanu Chowdhury, and Ruma Banerjee. "Importance of the Histidine Ligand to Coenzyme B12in the Reaction Catalyzed by Methylmalonyl-CoA Mutase." Journal of Biological Chemistry 277, no. 21 (March 13, 2002): 18523–27. http://dx.doi.org/10.1074/jbc.m111809200.
Повний текст джерелаBirch, A., A. Leiser, and J. A. Robinson. "Cloning, sequencing, and expression of the gene encoding methylmalonyl-coenzyme A mutase from Streptomyces cinnamonensis." Journal of Bacteriology 175, no. 11 (1993): 3511–19. http://dx.doi.org/10.1128/jb.175.11.3511-3519.1993.
Повний текст джерелаZhao, Ymin, Peter Such, and János Rétey. "Radical Intermediates in the Coenzyme B12 Dependent Methylmalonyl-CoA Mutase Reaction Shown by ESR Spectroscopy." Angewandte Chemie International Edition in English 31, no. 2 (February 1992): 215–16. http://dx.doi.org/10.1002/anie.199202151.
Повний текст джерелаAliarabi, H., S. Bisheh Sari, M. M. Tabatabaei, A. Ahmadi, P. Zamani, D. Alipour, and Z. Zamani. "Effect of cobalt supplementation on performance of Mehraban lambs." Proceedings of the British Society of Animal Science 2009 (April 2009): 167. http://dx.doi.org/10.1017/s1752756200030064.
Повний текст джерелаKumar, Neeraj, Shubin Liu, and Pawel M. Kozlowski. "Charge Separation Propensity of the Coenzyme B12–Tyrosine Complex in Adenosylcobalamin-Dependent Methylmalonyl–CoA Mutase Enzyme." Journal of Physical Chemistry Letters 3, no. 8 (April 9, 2012): 1035–38. http://dx.doi.org/10.1021/jz300102s.
Повний текст джерелаYamanishi, Mamoru, Tetyana Labunska, and Ruma Banerjee. "Mirror “Base-off” Conformation of Coenzyme B12in Human Adenosyltransferase and Its Downstream Target, Methylmalonyl-CoA Mutase." Journal of the American Chemical Society 127, no. 2 (January 2005): 526–27. http://dx.doi.org/10.1021/ja044365l.
Повний текст джерелаChowdhury, Shantanu, and Ruma Banerjee. "Role of the Dimethylbenzimidazole Tail in the Reaction Catalyzed by Coenzyme B12-Dependent Methylmalonyl-CoA Mutase†." Biochemistry 38, no. 46 (November 1999): 15287–94. http://dx.doi.org/10.1021/bi9914762.
Повний текст джерелаKorotkova, Natalia, Ludmila Chistoserdova, Vladimir Kuksa, and Mary E. Lidstrom. "Glyoxylate Regeneration Pathway in the Methylotroph Methylobacterium extorquens AM1." Journal of Bacteriology 184, no. 6 (March 15, 2002): 1750–58. http://dx.doi.org/10.1128/jb.184.6.1750-1758.2002.
Повний текст джерелаCordes, Thekla, and Christian M. Metallo. "Itaconate Alters Succinate and Coenzyme A Metabolism via Inhibition of Mitochondrial Complex II and Methylmalonyl-CoA Mutase." Metabolites 11, no. 2 (February 18, 2021): 117. http://dx.doi.org/10.3390/metabo11020117.
Повний текст джерелаGotoh, Kana, Yoko Nakajima, Go Tajima, Yuji Hotta, Tomoya Kataoka, Yoshihiro Kawade, Naruji Sugiyama, Tetsuya Ito, Kazunori Kimura, and Yasuhiro Maeda. "Assay for methylmalonyl coenzyme A mutase activity based on determination of succinyl coenzyme A by ultrahigh-performance liquid chromatography tandem mass spectrometry." Analytical and Bioanalytical Chemistry 407, no. 18 (May 28, 2015): 5281–86. http://dx.doi.org/10.1007/s00216-015-8753-8.
Повний текст джерелаMichenfelder, Martina, та János Rétey. "Methylmalonylcarba(dethia)-Coenzyme A as Substrate of the Coenzyme B12-Dependent Methylmalonyl-CoA Mutase: Enzymatic Rearrangement of aβ- to aγ-Keto Acid". Angewandte Chemie International Edition in English 25, № 4 (квітень 1986): 366–67. http://dx.doi.org/10.1002/anie.198603661.
Повний текст джерелаDong, Shoulian, Raghavakaimal Padmakumar, Ruma Banerjee, and Thomas G. Spiro. "Co−C Bond Activation in B12-Dependent Enzymes: Cryogenic Resonance Raman Studies of Methylmalonyl-Coenzyme A Mutase." Journal of the American Chemical Society 121, no. 30 (August 1999): 7063–70. http://dx.doi.org/10.1021/ja982753f.
Повний текст джерелаSmith, David M., Bernard T. Golding, and Leo Radom. "Facilitation of Enzyme-Catalyzed Reactions by Partial Proton Transfer: Application to Coenzyme-B12-Dependent Methylmalonyl-CoA Mutase." Journal of the American Chemical Society 121, no. 6 (February 1999): 1383–84. http://dx.doi.org/10.1021/ja983512a.
Повний текст джерелаChowdhury, Shantanu, and Ruma Banerjee. "Thermodynamic and Kinetic Characterization of Co−C Bond Homolysis Catalyzed by Coenzyme B12-Dependent Methylmalonyl-CoA Mutase†." Biochemistry 39, no. 27 (July 2000): 7998–8006. http://dx.doi.org/10.1021/bi992535e.
Повний текст джерелаHarrington, Dominic J. "Laboratory assessment of vitamin B12 status." Journal of Clinical Pathology 70, no. 2 (May 11, 2016): 168–73. http://dx.doi.org/10.1136/jclinpath-2015-203502.
Повний текст джерелаGhosh, Arghya Pratim, Megan J. Toda, and Pawel M. Kozlowski. "What Triggers the Cleavage of the Co–C5′ Bond in Coenzyme B12-Dependent Itaconyl-CoA Methylmalonyl-CoA Mutase?" ACS Catalysis 11, no. 13 (June 16, 2021): 7943–55. http://dx.doi.org/10.1021/acscatal.1c00291.
Повний текст джерелаMaiti, Nilesh, Lusiana Widjaja, and Ruma Banerjee. "Proton Transfer from Histidine 244 May Facilitate the 1,2 Rearrangement Reaction in Coenzyme B12-dependent Methylmalonyl-CoA Mutase." Journal of Biological Chemistry 274, no. 46 (November 12, 1999): 32733–37. http://dx.doi.org/10.1074/jbc.274.46.32733.
Повний текст джерелаGaire, D. "Comparison of two methods for the measurement of rat liver methylmalonyl-coenzyme A mutase activity: HPLC and radioisotopic assays." Journal of Nutritional Biochemistry 10, no. 1 (January 1999): 56–62. http://dx.doi.org/10.1016/s0955-2863(98)00083-7.
Повний текст джерелаChowdhury, Shantanu, Michael G. Thomas, Jorge C. Escalante-Semerena, and Ruma Banerjee. "The Coenzyme B12Analog 5′-Deoxyadenosylcobinamide-GDP Supports Catalysis by Methylmalonyl-CoA Mutase in the Absence of Trans-ligand Coordination." Journal of Biological Chemistry 276, no. 2 (October 12, 2000): 1015–19. http://dx.doi.org/10.1074/jbc.m006842200.
Повний текст джерелаDong, Shoulian, Raghavakaimal Padmakumar, Nilesh Maiti, Ruma Banerjee, and Thomas G. Spiro. "Resonance Raman Spectra Show That Coenzyme B12Binding to Methylmalonyl-Coenzyme A Mutase Changes the Corrin Ring Conformation but Leaves the Co−C Bond Essentially Unaffected." Journal of the American Chemical Society 120, no. 38 (September 1998): 9947–48. http://dx.doi.org/10.1021/ja981584w.
Повний текст джерелаMichenfelder, Martina, та János Rétey. "Methylmalonyl-cara(dethia)-Coenzym-A als Substrat der Coenzym-B,12-abhängigen Methylmalonyl-CoA-Mutase: Enzymatische Umlagerung einer β- zu einer γ-Ketosäure". Angewandte Chemie 98, № 4 (квітень 1986): 337–38. http://dx.doi.org/10.1002/ange.19860980408.
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