Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Hanan L. Messiha"'
Publikováno v:
ChemCatChem. 15
Publikováno v:
Ascue Avalos, G, Toogood, H, Tait, S, Messiha, H & Scrutton, N 2018, ' From bugs to bioplastics: Total (+)-dihydrocarvide biosynthesis by engineered Escherichia coli ', ChemBioChem: a European journal of chemical biology . https://doi.org/10.1002/cbic.201800606
Chembiochem
Chembiochem
The monoterpenoid lactone derivative (+)‐dihydrocarvide ((+)‐DHCD) can be polymerised to form shape‐memory polymers. Synthetic biology routes from simple, inexpensive carbon sources are an attractive, alternative route over chemical synthesis f
Publikováno v:
ACS synthetic biology. 10(2)
Conjugated alkenes such as dienes and polyenes have a range of applications as pharmaceutical agents and valuable building blocks in the polymer industry. Development of a renewable route to these compounds provides an alternative to fossil fuel deri
Autor:
Syed T. Ahmed, Gabriel A. Ascue Avalos, Adrian J. Mulholland, Reynier Suardíaz, Natalie Fey, Vijaykumar Karuppiah, Hanan L. Messiha, Stephen G. Yeates, Helen S. Toogood, Nigel S. Scrutton
Publikováno v:
Messiha, H L, Ahmed, S T, Karuppiah, V, Suardiaz, R, Ascue Avalos, G A, Fey, N, Yeates, S, Toogood, H S, Mulholland, A J & Scrutton, N S 2018, ' Biocatalytic Routes to Lactone Monomers for Polymer Production ', Biochemistry, vol. 57, no. 13, pp. 1997-2008 . https://doi.org/10.1021/acs.biochem.8b00169
Messiha, H L, Ahmed, S T, Karuppiah, V, Suardíaz, R, Ascue Avalos, G A, Fey, N, Yeates, S, Toogood, H S, Mulholland, A J & Scrutton, N S 2018, ' Biocatalytic routes to lactone monomers for polymer production ', Biochemistry, vol. 57, no. 13, pp. 1997-2008 . https://doi.org/10.1021/acs.biochem.8b00169
Messiha, H, Ahmed, S, Karuppiah, V, Suardiaz, R, Ascue Avalos, G, Fey, N, Yeates, S, Toogood, H, Mulholland, A J & Scrutton, N 2018, ' Biocatalytic Routes to Lactone Monomers for Polymer Production ', Biochemistry . https://doi.org/10.1021/acs.biochem.8b00169
Messiha, H L, Ahmed, S T, Karuppiah, V, Suardíaz, R, Ascue Avalos, G A, Fey, N, Yeates, S, Toogood, H S, Mulholland, A J & Scrutton, N S 2018, ' Biocatalytic routes to lactone monomers for polymer production ', Biochemistry, vol. 57, no. 13, pp. 1997-2008 . https://doi.org/10.1021/acs.biochem.8b00169
Messiha, H, Ahmed, S, Karuppiah, V, Suardiaz, R, Ascue Avalos, G, Fey, N, Yeates, S, Toogood, H, Mulholland, A J & Scrutton, N 2018, ' Biocatalytic Routes to Lactone Monomers for Polymer Production ', Biochemistry . https://doi.org/10.1021/acs.biochem.8b00169
Monoterpenoids offer potential as biocatalytically derived monomer feedstocks for high-performance renewable polymers. We describe a biocatalytic route to lactone monomers menthide and dihydrocarvide employing Baeyer-Villiger monooxygenases (BVMOs) f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a480a2e7ffdd2f827c476908d64730fe
https://research-information.bris.ac.uk/ws/files/155754971/BVMO_manuscript_biochemistry_12_03_18.pdf
https://research-information.bris.ac.uk/ws/files/155754971/BVMO_manuscript_biochemistry_12_03_18.pdf
Autor:
Hans V. Westerhoff, Barbara M. Bakker, Fred C. Boogerd, Hanan L. Messiha, Pedro Mendes, Frédéric Crémazy, Femke I. C. Mensonides
Publikováno v:
FEBS Letters, 587(17), 2860-2867. Wiley
FEBS Letters, 587(17), 2860-2867. Wiley-Blackwell
Mensonides, F I C, Bakker, B M, Cremazy, F, Messiha, H L, Mendes, P, Boogerd, F C & Westerhoff, H V 2013, ' A new regulatory principle for in vivo biochemistry : pleiotropic low affinity regulation by the adenine nucleotides--illustrated for the glycolytic enzymes of Saccharomyces cerevisiae ', FEBS Letters, vol. 587, no. 17, pp. 2860-2867 . https://doi.org/10.1016/j.febslet.2013.07.013
FEBS Letters, 587(17), 2860-2867. Elsevier
FEBS Letters, 587(17), 2860-2867. Wiley-Blackwell
Mensonides, F I C, Bakker, B M, Cremazy, F, Messiha, H L, Mendes, P, Boogerd, F C & Westerhoff, H V 2013, ' A new regulatory principle for in vivo biochemistry : pleiotropic low affinity regulation by the adenine nucleotides--illustrated for the glycolytic enzymes of Saccharomyces cerevisiae ', FEBS Letters, vol. 587, no. 17, pp. 2860-2867 . https://doi.org/10.1016/j.febslet.2013.07.013
FEBS Letters, 587(17), 2860-2867. Elsevier
Enzymology tends to focus on highly specific effects of substrates, allosteric modifiers, and products occurring at low concentrations, because these are most informative about the enzyme's catalytic mechanism. We hypothesized that at relatively high
Autor:
Norman W. Paton, Hanan L. Messiha, Olga Krebs, Heidrun Sauer-Danzwith, Isabel Rojas, Sylvestre Kengne, Pedro Mendes, Andreas Weidemann, Neil Swainston, Saqib Mir, Naglis Malys, Ulrike Wittig, Douglas B. Kell, Renate Kania, Kieran Smallbone, Wolfgang Müller, Martin Golebiewski
Publikováno v:
FEBS Journal. 277:3769-3779
A limited number of publicly available resources provide access to enzyme kinetic parameters. These have been compiled through manual data mining of published papers, not from the original, raw experimental data from which the parameters were calcula
Autor:
Evangelos Simeonidis, Catherine L. Winder, Hans V. Westerhoff, Hanan L. Messiha, Warwick B. Dunn, Frank J. Bruggeman, Malgorzata Adamczyk, Malkhey Verma
Publikováno v:
FEBS Letters, 583(24), 3882-3890
FEBS Letters, 583, 3882-3890. Elsevier
Westerhoff, H V, Winder, C, Messiha, H, Simeonidis, E, Adamczyk, M, Verma, M, Bruggeman, F J & Dunn, W 2009, ' Systems Biology: the elements and principles of life. ', FEBS Letters, vol. 583, pp. 3882-3890 . https://doi.org/10.1016/j.febslet.2009.11.018
FEBS Letters, 583, 3882-3890. Elsevier
Westerhoff, H V, Winder, C, Messiha, H, Simeonidis, E, Adamczyk, M, Verma, M, Bruggeman, F J & Dunn, W 2009, ' Systems Biology: the elements and principles of life. ', FEBS Letters, vol. 583, pp. 3882-3890 . https://doi.org/10.1016/j.febslet.2009.11.018
Systems Biology has a mission that puts it at odds with traditional paradigms of physics and molecular biology, such as the simplicity requested by Occam's razor and minimum energy/maximal efficiency. By referring to biochemical experiments on contro
Autor:
Gergely Katona, Selena G. Burgess, Stephen E. J. Rigby, Nigel S. Scrutton, David Leys, Hanan L. Messiha
Publikováno v:
Biochemistry. 47:5168-5181
We have used multiple solution state techniques and crystallographic analysis to investigate the importance of a putative transient interaction formed between Arg-alpha237 in electron transferring flavoprotein (ETF) and Tyr-442 in trimethylamine dehy
Autor:
Roger J, Kutta, Samantha J O, Hardman, Linus O, Johannissen, Bruno, Bellina, Hanan L, Messiha, Juan Manuel, Ortiz-Guerrero, Montserrat, Elías-Arnanz, S, Padmanabhan, Perdita, Barran, Nigel S, Scrutton, Alex R, Jones
Publikováno v:
Nature Communications
The coenzyme B12-dependent photoreceptor protein, CarH, is a bacterial transcriptional regulator that controls the biosynthesis of carotenoids in response to light. On binding of coenzyme B12 the monomeric apoprotein forms tetramers in the dark, whic
Publikováno v:
Messiha, HL, Wongnate, T, Chaiyen, P, Jones, A & Scrutton, NS 2015, ' Magnetic field effects as a result of the radical pair mechanism are unlikely in redox enzymes ', Journal of the Royal Society. Interface, vol. 12, 20141155, pp. 20141155 . https://doi.org/10.1098/rsif.2014.1155
Journal of the Royal Society Interface
Journal of the Royal Society Interface
Environmental exposure to electromagnetic fields is potentially carcinogenic. The radical pair mechanism is considered the most feasible mechanism of interaction between weak magnetic fields encountered in our environment and biochemical systems. Rad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8dcb55487a03592443f7bb04159b0ad5
https://www.research.manchester.ac.uk/portal/en/publications/magnetic-field-effects-as-a-result-of-the-radical-pair-mechanism-are-unlikely-in-redox-enzymes(1a6943d4-9c16-49bb-99ee-d1510f4fc0bc).html
https://www.research.manchester.ac.uk/portal/en/publications/magnetic-field-effects-as-a-result-of-the-radical-pair-mechanism-are-unlikely-in-redox-enzymes(1a6943d4-9c16-49bb-99ee-d1510f4fc0bc).html