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Showing 1 to 12 of 19 entries
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Model-Based Design of Biochemical Microreactors.

Frontiers in bioengineering and biotechnology

Elbinger T, Gahn M, Neuss-Radu M, Hante FM, Voll LM, Leugering G, Knabner P.
PMID: 26913283
Front Bioeng Biotechnol. 2016 Feb 15;4:13. doi: 10.3389/fbioe.2016.00013. eCollection 2016.

Mathematical modeling of biochemical pathways is an important resource in Synthetic Biology, as the predictive power of simulating synthetic pathways represents an important step in the design of synthetic metabolons. In this paper, we are concerned with the mathematical...

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Elbinger T, Gahn M, Neuss-Radu M, et al. Model-Based Design of Biochemical Microreactors. Front Bioeng Biotechnol. 2016;4:13doi: 10.3389/fbioe.2016.00013.
Elbinger, T., Gahn, M., Neuss-Radu, M., Hante, F. M., Voll, L. M., Leugering, G., & Knabner, P. (2016). Model-Based Design of Biochemical Microreactors. Frontiers in bioengineering and biotechnology, 413. https://doi.org/10.3389/fbioe.2016.00013
Elbinger, Tobias, et al. "Model-Based Design of Biochemical Microreactors." Frontiers in bioengineering and biotechnology vol. 4 (2016): 13. doi: https://doi.org/10.3389/fbioe.2016.00013
Elbinger T, Gahn M, Neuss-Radu M, Hante FM, Voll LM, Leugering G, Knabner P. Model-Based Design of Biochemical Microreactors. Front Bioeng Biotechnol. 2016 Feb 15;4:13. doi: 10.3389/fbioe.2016.00013. eCollection 2016. PMID: 26913283; PMCID: PMC4753381.
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Plant cell biology in the new millennium: new tools and new insights.

American journal of botany

Blancaflor EB, Gilroy S.
PMID: 11080104
Am J Bot. 2000 Nov;87(11):1547-60.

The highly regulated structural components of the plant cell form the basis of its function. It is becoming increasingly recognized that cellular components are ordered into regulatory units ranging from the multienzyme complexes that allow metabolic channeling during primary...

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Blancaflor EB, Gilroy S. Plant cell biology in the new millennium: new tools and new insights. Am J Bot. 2000;87(11):1547-60
Blancaflor, E. B., & Gilroy, S. (2000). Plant cell biology in the new millennium: new tools and new insights. American journal of botany, 87(11), 1547-60.
Blancaflor, E B, and Gilroy, S. "Plant cell biology in the new millennium: new tools and new insights." American journal of botany vol. 87,11 (2000): 1547-60.
Blancaflor EB, Gilroy S. Plant cell biology in the new millennium: new tools and new insights. Am J Bot. 2000 Nov;87(11):1547-60. PMID: 11080104.
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Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ.

Proceedings of the National Academy of Sciences of the United States of America

Suss KH, Arkona C, Manteuffel R, Adler K.
PMID: 11607406
Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5514-8. doi: 10.1073/pnas.90.12.5514.

Further evidence is provided that the Calvin cycle enzymes ribose-5-phosphate isomerase (EC 5.3.1.6), ribulose-5-phosphate kinase (Ru-5-P-K, EC 2.7.1.19), ribulose-1,5-bisphosphate carboxylase (RuP2Case, EC 4.1.1.39), glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12), sedoheptulose-1,7-bisphosphatase (Sed-1,7-bPase, EC 3.1.3.37), and electron transport protein ferredoxin-NADP+ reductase (FNR,...

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Suss KH, Arkona C, Manteuffel R, et al. Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ. Proc Natl Acad Sci U S A. 1993;90(12):5514-8doi: 10.1073/pnas.90.12.5514.
Suss, K. H., Arkona, C., Manteuffel, R., & Adler, K. (1993). Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ. Proceedings of the National Academy of Sciences of the United States of America, 90(12), 5514-8. https://doi.org/10.1073/pnas.90.12.5514
Suss, K H, et al. "Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ." Proceedings of the National Academy of Sciences of the United States of America vol. 90,12 (1993): 5514-8. doi: https://doi.org/10.1073/pnas.90.12.5514
Suss KH, Arkona C, Manteuffel R, Adler K. Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ. Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5514-8. doi: 10.1073/pnas.90.12.5514. PMID: 11607406; PMCID: PMC46751.
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Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts.

Photosynthesis research

Balmer Y, Koller A, Val GD, Schürmann P, Buchanan BB.
PMID: 16328793
Photosynth Res. 2004;79(3):275-80. doi: 10.1023/B:PRES.0000017207.88257.d4.

The ability of thioredoxin f to form an electrostatic (non-covalent) complex, earlier found with fructose-1,6-bisphosphatase, was extended to include 27 previously unrecognized proteins functional in 11 processes of chloroplasts. The proteins were identified by combining thioredoxin f affinity chromatography...

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Balmer Y, Koller A, Val GD, et al. Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynth Res. 2004;79(3):275-80doi: 10.1023/B:PRES.0000017207.88257.d4.
Balmer, Y., Koller, A., Val, G. D., Schürmann, P., & Buchanan, B. B. (2004). Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynthesis research, 79(3), 275-80. https://doi.org/10.1023/B:PRES.0000017207.88257.d4
Balmer, Yves, et al. "Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts." Photosynthesis research vol. 79,3 (2004): 275-80. doi: https://doi.org/10.1023/B:PRES.0000017207.88257.d4
Balmer Y, Koller A, Val GD, Schürmann P, Buchanan BB. Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynth Res. 2004;79(3):275-80. doi: 10.1023/B:PRES.0000017207.88257.d4. PMID: 16328793.
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Membrane anchoring facilitates colocalization of enzymes in plant cytochrome P450 redox systems.

Communications biology

Laursen T, Lam HYM, Sørensen KK, Tian P, Hansen CC, Groves JT, Jensen KJ, Christensen SM.
PMID: 34504298
Commun Biol. 2021 Sep 09;4(1):1057. doi: 10.1038/s42003-021-02604-1.

Plant metabolism depends on cascade reactions mediated by dynamic enzyme assemblies known as metabolons. In this context, the cytochrome P450 (P450) superfamily catalyze key reactions underpinning the unique diversity of bioactive compounds. In contrast to their soluble bacterial counterparts,...

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Laursen T, Lam HYM, Sørensen KK, et al. Membrane anchoring facilitates colocalization of enzymes in plant cytochrome P450 redox systems. Commun Biol. 2021;4(1):1057doi: 10.1038/s42003-021-02604-1.
Laursen, T., Lam, H. Y. M., Sørensen, K. K., Tian, P., Hansen, C. C., Groves, J. T., Jensen, K. J., & Christensen, S. M. (2021). Membrane anchoring facilitates colocalization of enzymes in plant cytochrome P450 redox systems. Communications biology, 4(1), 1057. https://doi.org/10.1038/s42003-021-02604-1
Laursen, Tomas, et al. "Membrane anchoring facilitates colocalization of enzymes in plant cytochrome P450 redox systems." Communications biology vol. 4,1 (2021): 1057. doi: https://doi.org/10.1038/s42003-021-02604-1
Laursen T, Lam HYM, Sørensen KK, Tian P, Hansen CC, Groves JT, Jensen KJ, Christensen SM. Membrane anchoring facilitates colocalization of enzymes in plant cytochrome P450 redox systems. Commun Biol. 2021 Sep 09;4(1):1057. doi: 10.1038/s42003-021-02604-1. PMID: 34504298; PMCID: PMC8429664.
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Processive Enzymes Kept on a Leash: How Cellulase Activity in Multienzyme Complexes Directs Nanoscale Deconstruction of Cellulose.

ACS catalysis

Zajki-Zechmeister K, Kaira GS, Eibinger M, Seelich K, Nidetzky B.
PMID: 34777910
ACS Catal. 2021 Nov 05;11(21):13530-13542. doi: 10.1021/acscatal.1c03465. Epub 2021 Oct 25.

Biological deconstruction of polymer materials gains efficiency from the spatiotemporally coordinated action of enzymes with synergetic function in polymer chain depolymerization. To perpetuate enzyme synergy on a solid substrate undergoing deconstruction, the overall attack must alternate between focusing the...

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Zajki-Zechmeister K, Kaira GS, Eibinger M, et al. Processive Enzymes Kept on a Leash: How Cellulase Activity in Multienzyme Complexes Directs Nanoscale Deconstruction of Cellulose. ACS Catal. 2021;11(21):13530-13542doi: 10.1021/acscatal.1c03465.
Zajki-Zechmeister, K., Kaira, G. S., Eibinger, M., Seelich, K., & Nidetzky, B. (2021). Processive Enzymes Kept on a Leash: How Cellulase Activity in Multienzyme Complexes Directs Nanoscale Deconstruction of Cellulose. ACS catalysis, 11(21), 13530-13542. https://doi.org/10.1021/acscatal.1c03465
Zajki-Zechmeister, Krisztina, et al. "Processive Enzymes Kept on a Leash: How Cellulase Activity in Multienzyme Complexes Directs Nanoscale Deconstruction of Cellulose." ACS catalysis vol. 11,21 (2021): 13530-13542. doi: https://doi.org/10.1021/acscatal.1c03465
Zajki-Zechmeister K, Kaira GS, Eibinger M, Seelich K, Nidetzky B. Processive Enzymes Kept on a Leash: How Cellulase Activity in Multienzyme Complexes Directs Nanoscale Deconstruction of Cellulose. ACS Catal. 2021 Nov 05;11(21):13530-13542. doi: 10.1021/acscatal.1c03465. Epub 2021 Oct 25. PMID: 34777910; PMCID: PMC8576811.
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Metabolic compartmentation - a system level property of muscle cells: real problems of diffusion in living cells.

International journal of molecular sciences

Saks V, Beraud N, Wallimann T.
PMID: 19325782
Int J Mol Sci. 2008 May;9(5):751-67. doi: 10.3390/ijms9050751. Epub 2008 May 09.

Problems of quantitative investigation of intracellular diffusion and compartmentation of metabolites are analyzed. Principal controversies in recently published analyses of these problems for the living cells are discussed. It is shown that the formal theoretical analysis of diffusion of...

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Saks V, Beraud N, Wallimann T. Metabolic compartmentation - a system level property of muscle cells: real problems of diffusion in living cells. Int J Mol Sci. 2008;9(5):751-67doi: 10.3390/ijms9050751.
Saks, V., Beraud, N., & Wallimann, T. (2008). Metabolic compartmentation - a system level property of muscle cells: real problems of diffusion in living cells. International journal of molecular sciences, 9(5), 751-67. https://doi.org/10.3390/ijms9050751
Saks, Valdur, et al. "Metabolic compartmentation - a system level property of muscle cells: real problems of diffusion in living cells." International journal of molecular sciences vol. 9,5 (2008): 751-67. doi: https://doi.org/10.3390/ijms9050751
Saks V, Beraud N, Wallimann T. Metabolic compartmentation - a system level property of muscle cells: real problems of diffusion in living cells. Int J Mol Sci. 2008 May;9(5):751-67. doi: 10.3390/ijms9050751. Epub 2008 May 09. PMID: 19325782; PMCID: PMC2635703.
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Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis.

Plant physiology

Ewald R, Hoffmann C, Florian A, Neuhaus E, Fernie AR, Bauwe H.
PMID: 24872381
Plant Physiol. 2014 Jul;165(3):978-990. doi: 10.1104/pp.114.238311. Epub 2014 May 28.

Prosthetic lipoyl groups are required for the function of several essential multienzyme complexes, such as pyruvate dehydrogenase (PDH), α-ketoglutarate dehydrogenase (KGDH), and the glycine cleavage system (glycine decarboxylase [GDC]). How these proteins are lipoylated has been extensively studied in...

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Ewald R, Hoffmann C, Florian A, et al. Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis. Plant Physiol. 2014;165(3):978-990doi: 10.1104/pp.114.238311.
Ewald, R., Hoffmann, C., Florian, A., Neuhaus, E., Fernie, A. R., & Bauwe, H. (2014). Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis. Plant physiology, 165(3), 978-990. https://doi.org/10.1104/pp.114.238311
Ewald, Ralph, et al. "Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis." Plant physiology vol. 165,3 (2014): 978-990. doi: https://doi.org/10.1104/pp.114.238311
Ewald R, Hoffmann C, Florian A, Neuhaus E, Fernie AR, Bauwe H. Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis. Plant Physiol. 2014 Jul;165(3):978-990. doi: 10.1104/pp.114.238311. Epub 2014 May 28. PMID: 24872381; PMCID: PMC4081350.
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Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme.

Journal of biochemical and pharmacological research

Yan LJ, Thangthaeng N, Sumien N, Forster MJ.
PMID: 23646291
J Biochem Pharmacol Res. 2013 Mar;1(1):30-42.

Dihydrolipoamide dehydrogenase (DLDH) is a multifunctional oxidoreductase and is well known as an essential component of four mammalian mitochondrial multienzyme complexes: pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, branched chain α-keto acid dehydrogenase, and the glycine cleavage system. However, existence of extracellular...

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Yan LJ, Thangthaeng N, Sumien N, et al. Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme. J Biochem Pharmacol Res. 2013;1(1):30-42
Yan, L. J., Thangthaeng, N., Sumien, N., & Forster, M. J. (2013). Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme. Journal of biochemical and pharmacological research, 1(1), 30-42.
Yan, Liang-Jun, et al. "Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme." Journal of biochemical and pharmacological research vol. 1,1 (2013): 30-42.
Yan LJ, Thangthaeng N, Sumien N, Forster MJ. Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme. J Biochem Pharmacol Res. 2013 Mar;1(1):30-42. PMID: 23646291; PMCID: PMC3641859.
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How evolution dismantles and reassembles multienzyme complexes.

Proceedings of the National Academy of Sciences of the United States of America

Mattevi A.
PMID: 34996854
Proc Natl Acad Sci U S A. 2022 Jan 04;119(1). doi: 10.1073/pnas.2120286118. Epub 2021 Dec 22.

No abstract available.

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Mattevi A. How evolution dismantles and reassembles multienzyme complexes. Proc Natl Acad Sci U S A. 2021;119(1)doi: 10.1073/pnas.2120286118.
Mattevi, A. (2022). How evolution dismantles and reassembles multienzyme complexes. Proceedings of the National Academy of Sciences of the United States of America, 119(1), . https://doi.org/10.1073/pnas.2120286118
Mattevi, Andrea. "How evolution dismantles and reassembles multienzyme complexes." Proceedings of the National Academy of Sciences of the United States of America vol. 119,1 (2022). doi: https://doi.org/10.1073/pnas.2120286118
Mattevi A. How evolution dismantles and reassembles multienzyme complexes. Proc Natl Acad Sci U S A. 2022 Jan 04;119(1). doi: 10.1073/pnas.2120286118. Epub 2021 Dec 22. PMID: 34996854.
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How evolution dismantles and reassembles multienzyme complexes.

Proceedings of the National Academy of Sciences of the United States of America

Mattevi A.
PMID: 34996854
Proc Natl Acad Sci U S A. 2022 Jan 04;119(1). doi: 10.1073/pnas.2120286118. Epub 2021 Dec 22.

No abstract available.

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Mattevi A. How evolution dismantles and reassembles multienzyme complexes. Proc Natl Acad Sci U S A. 2021;119(1)doi: 10.1073/pnas.2120286118.
Mattevi, A. (2022). How evolution dismantles and reassembles multienzyme complexes. Proceedings of the National Academy of Sciences of the United States of America, 119(1), . https://doi.org/10.1073/pnas.2120286118
Mattevi, Andrea. "How evolution dismantles and reassembles multienzyme complexes." Proceedings of the National Academy of Sciences of the United States of America vol. 119,1 (2022). doi: https://doi.org/10.1073/pnas.2120286118
Mattevi A. How evolution dismantles and reassembles multienzyme complexes. Proc Natl Acad Sci U S A. 2022 Jan 04;119(1). doi: 10.1073/pnas.2120286118. Epub 2021 Dec 22. PMID: 34996854.
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Production of Biomass-Degrading Multienzyme Complexes under Solid-State Fermentation of Soybean Meal Using a Bioreactor.

Enzyme research

Vitcosque GL, Fonseca RF, Rodríguez-Zúñiga UF, Bertucci Neto V, Couri S, Farinas CS.
PMID: 23365723
Enzyme Res. 2012;2012:248983. doi: 10.1155/2012/248983. Epub 2012 Dec 29.

Biomass-degrading enzymes are one of the most costly inputs affecting the economic viability of the biochemical route for biomass conversion into biofuels. This work evaluates the effects of operational conditions on biomass-degrading multienzyme production by a selected strain of...

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Vitcosque GL, Fonseca RF, Rodríguez-Zúñiga UF, et al. Production of Biomass-Degrading Multienzyme Complexes under Solid-State Fermentation of Soybean Meal Using a Bioreactor. Enzyme Res. 2012;2012:248983doi: 10.1155/2012/248983.
Vitcosque, G. L., Fonseca, R. F., Rodríguez-Zúñiga, U. F., Bertucci Neto, V., Couri, S., & Farinas, C. S. (2012). Production of Biomass-Degrading Multienzyme Complexes under Solid-State Fermentation of Soybean Meal Using a Bioreactor. Enzyme research, 2012248983. https://doi.org/10.1155/2012/248983
Vitcosque, Gabriela L, et al. "Production of Biomass-Degrading Multienzyme Complexes under Solid-State Fermentation of Soybean Meal Using a Bioreactor." Enzyme research vol. 2012 (2012): 248983. doi: https://doi.org/10.1155/2012/248983
Vitcosque GL, Fonseca RF, Rodríguez-Zúñiga UF, Bertucci Neto V, Couri S, Farinas CS. Production of Biomass-Degrading Multienzyme Complexes under Solid-State Fermentation of Soybean Meal Using a Bioreactor. Enzyme Res. 2012;2012:248983. doi: 10.1155/2012/248983. Epub 2012 Dec 29. PMID: 23365723; PMCID: PMC3544265.
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