Journal articles on the topic 'Coenzyme enzyme complex'
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Tsai, C. Stan, and D. J. Senior. "Dual coenzyme activities of high-Km aldehyde dehydrogenase from rat liver mitochondria." Biochemistry and Cell Biology 68, no. 4 (April 1, 1990): 751–57. http://dx.doi.org/10.1139/o90-108.
Full textSperanza, Giovanna, Wolfgang Buckel, and Bernard T. Golding. "CoenzymeB12-dependent enzymatic dehydration of 1,2-diols: simple reaction, complex mechanism!" Journal of Porphyrins and Phthalocyanines 08, no. 03 (March 2004): 290–300. http://dx.doi.org/10.1142/s1088424604000271.
Full textEhebauer, Matthias, Madhan Anandhakrishnan, Michael Zimmermann, Elke Noens, Arjen Jakobi, Carsten Sachse, Uwe Sauer, and Matthias Wilmanns. "AccD1 And AccA1 from M. tuberculosis form A dodecameric MCC-type holo complex." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C429. http://dx.doi.org/10.1107/s2053273314095709.
Full textTeixido, Francisco, Dolores De Arriaga, Félix Busto, and Joaquin Soler. "Cytoplasmic malate dehydrogenase from Phycomyces blakesleeanus: Kinetics and mechanism." Canadian Journal of Biochemistry and Cell Biology 63, no. 10 (October 1, 1985): 1097–105. http://dx.doi.org/10.1139/o85-137.
Full textKang, Lin-Woo, Sandra B. Gabelli, Mario A. Bianchet, Wen Lian Xu, Maurice J. Bessman, and L. Mario Amzel. "Structure of a Coenzyme A Pyrophosphatase from Deinococcus radiodurans: a Member of the Nudix Family." Journal of Bacteriology 185, no. 14 (July 15, 2003): 4110–18. http://dx.doi.org/10.1128/jb.185.14.4110-4118.2003.
Full textBell, E. T., C. LiMuti, C. L. Renz, and J. E. Bell. "Negative co-operativity in glutamate dehydrogenase. Involvement of the 2-position in glutamate in the induction of conformational changes." Biochemical Journal 225, no. 1 (January 1, 1985): 209–17. http://dx.doi.org/10.1042/bj2250209.
Full textFriedmann, Silke, Astrid Steindorf, Birgit E. Alber, and Georg Fuchs. "Properties of Succinyl-Coenzyme A:l-Malate Coenzyme A Transferase and Its Role in the Autotrophic 3-Hydroxypropionate Cycle of Chloroflexus aurantiacus." Journal of Bacteriology 188, no. 7 (April 1, 2006): 2646–55. http://dx.doi.org/10.1128/jb.188.7.2646-2655.2006.
Full textLeskovac, Vladimir, Svetlana Trivic, and Draginja Pericin. "Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalysed reactions." Journal of the Serbian Chemical Society 68, no. 2 (2003): 77–84. http://dx.doi.org/10.2298/jsc0302077l.
Full textWinberg, J. O., and J. S. McKinley-McKee. "Drosophila melanogaster alcohol dehydrogenase: product-inhibition studies." Biochemical Journal 301, no. 3 (August 1, 1994): 901–9. http://dx.doi.org/10.1042/bj3010901.
Full textStiborová, Marie, and Sylva Leblová. "Mechanism of action of heavy metals, S-triazine herbicides and nitrates on alcohol dehydrogenase from rape." Collection of Czechoslovak Chemical Communications 51, no. 8 (1986): 1781–88. http://dx.doi.org/10.1135/cccc19861781.
Full textGriffin, Joanna, and Paul C. Engel. "The –SH Protection Method for Determining Accurate Kd Values for Enzyme-Coenzyme Complexes of NAD+-Dependent Glutamate Dehydrogenase and Engineered Mutants: Evidence for Nonproductive NADPH Complexes." Enzyme Research 2010 (June 29, 2010): 1–5. http://dx.doi.org/10.4061/2010/951472.
Full textGrishin, Andrey M., Eunice Ajamian, Linhua Zhang, and Miroslaw Cygler. "Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of theEscherichia coliphenylacetyl-coenzyme A oxygenase complex." Acta Crystallographica Section F Structural Biology and Crystallization Communications 66, no. 9 (August 26, 2010): 1045–49. http://dx.doi.org/10.1107/s174430911002748x.
Full textHidalgo-Gutiérrez, Agustín, Pilar González-García, María Elena Díaz-Casado, Eliana Barriocanal-Casado, Sergio López-Herrador, Catarina M. Quinzii, and Luis C. López. "Metabolic Targets of Coenzyme Q10 in Mitochondria." Antioxidants 10, no. 4 (March 26, 2021): 520. http://dx.doi.org/10.3390/antiox10040520.
Full textZhang, Yanli, Linley R. Schofield, Carrie Sang, Debjit Dey, and Ron S. Ronimus. "Expression, Purification, and Characterization of (R)-Sulfolactate Dehydrogenase (ComC) from the Rumen MethanogenMethanobrevibacter milleraeSM9." Archaea 2017 (2017): 1–6. http://dx.doi.org/10.1155/2017/5793620.
Full textKuchmenko, E. B., D. N. Petukhov, G. V. Donchenko, L. S. Mkhitaryan, S. V. Tymoshchuk, N. A. Strutynskaya, G. L. Vavilova, and V. F. Sagach. "Effect of complexes of precursors and modulators of coenzyme q biosynthesis on functional state of old rats' heart mitochondria." Biomeditsinskaya Khimiya 56, no. 2 (2010): 244–56. http://dx.doi.org/10.18097/pbmc20105602244.
Full textShima, Seigo, Gangfeng Huang, Tristan Wagner, and Ulrich Ermler. "Structural Basis of Hydrogenotrophic Methanogenesis." Annual Review of Microbiology 74, no. 1 (September 8, 2020): 713–33. http://dx.doi.org/10.1146/annurev-micro-011720-122807.
Full textNEUHAUSER, Wilfried, Dietmar HALTRICH, Klaus D. KULBE, and Bernd NIDETZKY. "NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis: Isolation, characterization and biochemical properties of the enzyme." Biochemical Journal 326, no. 3 (September 15, 1997): 683–92. http://dx.doi.org/10.1042/bj3260683.
Full textMeikle, P. J., A. M. Whittle, and J. J. Hopwood. "Human acetyl-coenzyme A:α-glucosaminide N-acetyltransferase. Kinetic characterization and mechanistic interpretation." Biochemical Journal 308, no. 1 (May 15, 1995): 327–33. http://dx.doi.org/10.1042/bj3080327.
Full textAl-Kassim, Loola S., and C. Stan Tsai. "Purification and kinetic characterization of pickerel liver alcohol dehydrogenase with dual coenzyme specificity." Biochemistry and Cell Biology 71, no. 9-10 (September 1, 1993): 421–26. http://dx.doi.org/10.1139/o93-062.
Full textGarcía-Muriana, Francisco J., María C. Alvarez-Ossorioa, María M. Sánchez-Garcés, F. de la Rosa, and Angel M. Relimpio. "Further Characterization of Aspartate Aminotransferase from Haloferax mediterranei: Pyridoxal Phosphate as Coenzyme and Inhibitor." Zeitschrift für Naturforschung C 50, no. 3-4 (April 1, 1995): 241–47. http://dx.doi.org/10.1515/znc-1995-3-413.
Full textSmith, Clyde A., Marta Toth, Thomas M. Weiss, Hilary Frase, and Sergei B. Vakulenko. "Structure of the bifunctional aminoglycoside-resistance enzyme AAC(6′)-Ie-APH(2′′)-Ia revealed by crystallographic and small-angle X-ray scattering analysis." Acta Crystallographica Section D Biological Crystallography 70, no. 10 (September 27, 2014): 2754–64. http://dx.doi.org/10.1107/s1399004714017635.
Full textScott, A. Ian, and Charles A. Roessner. "Recent discoveries in the pathways to cobalamin (coenzyme B12) achieved through chemistry and biology." Pure and Applied Chemistry 79, no. 12 (January 1, 2007): 2179–88. http://dx.doi.org/10.1351/pac200779122179.
Full textCassetta, Alberto, Ivet Krastanova, Katja Kristan, Mojca Brunskole Švegelj, Doriano Lamba, Tea Lanišnik Rižner, and Jure Stojan. "Insights into subtle conformational differences in the substrate-binding loop of fungal 17β-hydroxysteroid dehydrogenase: a combined structural and kinetic approach." Biochemical Journal 441, no. 1 (December 14, 2011): 151–60. http://dx.doi.org/10.1042/bj20110567.
Full textWang, Shuning, Haiyan Huang, Johanna Moll, and Rudolf K. Thauer. "NADP+ Reduction with Reduced Ferredoxin and NADP+ Reduction with NADH Are Coupled via an Electron-Bifurcating Enzyme Complex in Clostridium kluyveri." Journal of Bacteriology 192, no. 19 (July 30, 2010): 5115–23. http://dx.doi.org/10.1128/jb.00612-10.
Full textChase, T. "Mannitol-1-phosphate dehydrogenase of Escherichia coli Chemical properties and binding of substrates." Biochemical Journal 239, no. 2 (October 15, 1986): 435–43. http://dx.doi.org/10.1042/bj2390435.
Full textMakukh, Y. M., T. M. Gryvul, A. Ya Krasnevich, and D. S. Vignan. "Aldosereductase: structure, mechanism of action, biological role and functioning according to normo and hyperglycemia." Scientific Messenger of LNU of Veterinary Medicine and Biotechnologies 22, no. 99 (October 28, 2020): 125–42. http://dx.doi.org/10.32718/nvlvet9920.
Full textLawrence, Sarah H., and James G. Ferry. "Steady-State Kinetic Analysis of Phosphotransacetylase from Methanosarcina thermophila." Journal of Bacteriology 188, no. 3 (February 1, 2006): 1155–58. http://dx.doi.org/10.1128/jb.188.3.1155-1158.2006.
Full textGago, Gabriela, Daniel Kurth, Lautaro Diacovich, Shiou-Chuan Tsai, and Hugo Gramajo. "Biochemical and Structural Characterization of an Essential Acyl Coenzyme A Carboxylase from Mycobacterium tuberculosis." Journal of Bacteriology 188, no. 2 (January 15, 2006): 477–86. http://dx.doi.org/10.1128/jb.188.2.477-486.2006.
Full textKumar, 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.
Full textRyle, C. M., and K. F. Tipton. "Kinetic studies with the low-Km aldehyde reductase from ox brain." Biochemical Journal 227, no. 2 (April 15, 1985): 621–27. http://dx.doi.org/10.1042/bj2270621.
Full textJohnson, Celeste L. V., Marian L. Buszko, and Thomas A. Bobik. "Purification and Initial Characterization of the Salmonella enterica PduO ATP:Cob(I)alamin Adenosyltransferase." Journal of Bacteriology 186, no. 23 (December 1, 2004): 7881–87. http://dx.doi.org/10.1128/jb.186.23.7881-7887.2004.
Full textBarthová, Jana, Irena Hulová, and Miroslava Birčáková. "Essential Arginine Residues in Lactate Dehydrogenase from Germinating Soybean." Collection of Czechoslovak Chemical Communications 59, no. 2 (1994): 467–72. http://dx.doi.org/10.1135/cccc19940467.
Full textPETSCHACHER, Barbara, Stefan LEITGEB, Kathryn L. KAVANAGH, David K. WILSON, and Bernd NIDETZKY. "The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography." Biochemical Journal 385, no. 1 (December 14, 2004): 75–83. http://dx.doi.org/10.1042/bj20040363.
Full textTjhin, Erick T., Vanessa M. Howieson, Christina Spry, Giel G. van Dooren, and Kevin J. Saliba. "A novel heteromeric pantothenate kinase complex in apicomplexan parasites." PLOS Pathogens 17, no. 7 (July 29, 2021): e1009797. http://dx.doi.org/10.1371/journal.ppat.1009797.
Full textMiller, Tarryn E., Thomas Beneyton, Thomas Schwander, Christoph Diehl, Mathias Girault, Richard McLean, Tanguy Chotel, et al. "Light-powered CO2 fixation in a chloroplast mimic with natural and synthetic parts." Science 368, no. 6491 (May 7, 2020): 649–54. http://dx.doi.org/10.1126/science.aaz6802.
Full textBrinsmade, Shaun R., Tenzin Paldon, and Jorge C. Escalante-Semerena. "Minimal Functions and Physiological Conditions Required for Growth of Salmonella enterica on Ethanolamine in the Absence of the Metabolosome." Journal of Bacteriology 187, no. 23 (December 1, 2005): 8039–46. http://dx.doi.org/10.1128/jb.187.23.8039-8046.2005.
Full textKeep, 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.
Full textLowe, D. M., and P. K. Tubbs. "3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver. Properties of its acetyl derivative." Biochemical Journal 227, no. 2 (April 15, 1985): 601–7. http://dx.doi.org/10.1042/bj2270601.
Full textPlapp, Bryce V., David C. Sogin, Robert T. Dworschack, David P. Bohlken, Christoph Woenckhaus, and Reinhard Jeck. "Kinetics and native and modified liver alcohol dehydrogenase with coenzyme analogs: isomerization of enzyme-nicotinamide adenine dinucleotide complex." Biochemistry 25, no. 19 (September 23, 1986): 5396–402. http://dx.doi.org/10.1021/bi00367a008.
Full textLeutwein, Christina, and Johann Heider. "Succinyl-CoA:(R)-Benzylsuccinate CoA-Transferase: an Enzyme of the Anaerobic Toluene Catabolic Pathway in Denitrifying Bacteria." Journal of Bacteriology 183, no. 14 (July 15, 2001): 4288–95. http://dx.doi.org/10.1128/jb.183.14.4288-4295.2001.
Full textBartucci, Roberta, Anna Salvati, Peter Olinga, and Ykelien L. Boersma. "Vanin 1: Its Physiological Function and Role in Diseases." International Journal of Molecular Sciences 20, no. 16 (August 9, 2019): 3891. http://dx.doi.org/10.3390/ijms20163891.
Full textTimofeev, Vladimir, Evgenia Smirnova, Larisa Chupova, Roman Esipov, and Inna Kuranova. "X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction." Acta Crystallographica Section D Biological Crystallography 68, no. 12 (November 9, 2012): 1660–70. http://dx.doi.org/10.1107/s0907444912040206.
Full textGonzález, Javier M., Ricardo Marti-Arbona, Julian C. H. Chen, Brian Broom-Peltz, and Clifford J. Unkefer. "Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase." Acta Crystallographica Section F Structural Biology Communications 74, no. 10 (September 19, 2018): 610–16. http://dx.doi.org/10.1107/s2053230x18011809.
Full textSong, Haigang, Hoi Pang Sung, Yuk Sing Tse, Ming Jiang, and Zhihong Guo. "Ligand-dependent active-site closure revealed in the crystal structure ofMycobacterium tuberculosisMenB complexed with product analogues." Acta Crystallographica Section D Biological Crystallography 70, no. 11 (October 23, 2014): 2959–69. http://dx.doi.org/10.1107/s1399004714019440.
Full textJun, A. S., I. A. Trounce, M. D. Brown, J. M. Shoffner, and D. C. Wallace. "Use of transmitochondrial cybrids to assign a complex I defect to the mitochondrial DNA-encoded NADH dehydrogenase subunit 6 gene mutation at nucleotide pair 14459 that causes Leber hereditary optic neuropathy and dystonia." Molecular and Cellular Biology 16, no. 3 (March 1996): 771–77. http://dx.doi.org/10.1128/mcb.16.3.771.
Full textSkursk, Ladislav, Miroslav Řezáĉ, Allah Nawaz Khan, Lukáŝ Žídek, and Jaroslav Roĉek. "Hydroperoxide Inhibitor of Horse Liver Alcohol Dehydrogenase Activity, Tightly Bound to the Enzyme-Nad+Complex, Characteristically Degrades the Coenzyme." Journal of Enzyme Inhibition 6, no. 3 (January 1992): 211–22. http://dx.doi.org/10.3109/14756369209020171.
Full textKeinanen, T. A., T. Hyvonen, J. Vepsalainen, L. Alhonen, A. R. Khomutov, and J. Janne. "Stable analogues of coenzyme-substrate complex of spermidine/spermine-N 1-acetyltransferase reaction. Synthesis and interaction with the enzyme." Russian Journal of Bioorganic Chemistry 40, no. 2 (March 2014): 155–61. http://dx.doi.org/10.1134/s1068162014020071.
Full textBohren, K. M., J. P. von Wartburg, and B. Wermuth. "Kinetics of carbonyl reductase from human brain." Biochemical Journal 244, no. 1 (May 15, 1987): 165–71. http://dx.doi.org/10.1042/bj2440165.
Full textKirilenko, Bogdan M., Lee R. Hagey, Stephen Barnes, Charles N. Falany, and Michael Hiller. "Evolutionary Analysis of Bile Acid-Conjugating Enzymes Reveals a Complex Duplication and Reciprocal Loss History." Genome Biology and Evolution 11, no. 11 (October 31, 2019): 3256–68. http://dx.doi.org/10.1093/gbe/evz238.
Full textWang, Lei, and K. M. J. Menon. "Regulation of Luteinizing Hormone/Chorionic Gonadotropin Receptor Messenger Ribonucleic Acid Expression in the Rat Ovary: Relationship to Cholesterol Metabolism." Endocrinology 146, no. 1 (January 1, 2005): 423–31. http://dx.doi.org/10.1210/en.2004-0805.
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