Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Andrew C. Muscroft-Taylor"'
Autor:
Jenna M. Gilkes, Rebekah A. Frampton, Amanda J. Board, André O. Hudson, Thomas G. Price, Deborah L. Crittenden, Andrew C. Muscroft-Taylor, Campbell R. Sheen, Grant R. Smith, Renwick C.J. Dobson
The effect of population bottlenecks and genome reduction on enzyme function is poorly understood. ‘CandidatusLiberibacter solanacearum’ is a bacterium with a reduced genome that is transmitted vertically to the egg of an infected psyllid—a pop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4ae563f9989df70e9064ff8f57b7f708
https://doi.org/10.1101/2023.04.17.537279
https://doi.org/10.1101/2023.04.17.537279
Autor:
Michael J. Currie, Phillip M. Rendle, Lavanyaa Manjunath, Ramaswamy Subramanian, Christopher R Horne, Antony J. Fairbanks, Andrew C. Muscroft-Taylor, Renwick C. J. Dobson, Rachel A. North, Rosmarie Friemann
Publikováno v:
The Journal of Biological Chemistry
There are five known general catalytic mechanisms used by enzymes to catalyze carbohydrate epimerization. The amino sugar epimerase N-acetylmannosamine-6-phosphate 2-epimerase (NanE) has been proposed to use a deprotonation–reprotonation mechanism,
Autor:
Gayan Abeysekera, Renwick C. J. Dobson, Andrew C. Muscroft-Taylor, Michael J. Love, Craig Billington
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1868(1)
Bacteriophage endolysins have the potential to be a long-term antibacterial replacement for antibiotics. The exogenous application of endolysins on some bacteria results in rapid cell lysis. The prospects for endolysins are furthered by the ability t
Autor:
Weixiao Yuan Wahlgren, Rachel A. North, S. Ramaswamy, Christopher R Horne, Daniela M. Remus, James S Davies, Renwick C. J. Dobson, Rosmarie Friemann, Andrew C. Muscroft-Taylor, Parveen Goyal
Publikováno v:
Biophysical reviews. 10(2)
Eukaryotic cell surfaces are decorated with a complex array of glycoconjugates that are usually capped with sialic acids, a large family of over 50 structurally distinct nine-carbon amino sugars, the most common member of which is N-acetylneuraminic
Elucidation of the biological roles and more detailed structure–function relationships of human milk oligosaccharides (HMOs) requires access to homogeneous, defined HMO samples. Various approaches, including chemical synthesis, enzymatic/chemoenzym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8f599b8558675e97370d184d18389d46
https://doi.org/10.1016/b978-0-12-802725-7.00009-9
https://doi.org/10.1016/b978-0-12-802725-7.00009-9
Autor:
Antony J. Fairbanks, Andrew C. Muscroft-Taylor, F. Grant Pearce, Renwick C. J. Dobson, Andrew J. Watson, Rachel A. North, Rosmarie Friemann
Publikováno v:
FEBS letters. 590(23)
N-Acetylneuraminate lyase is the first committed enzyme in the degradation of sialic acid by bacterial pathogens. In this study, we analysed the kinetic parameters of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus (MRSA).
Publikováno v:
Biochimie. 92:254-262
Thermodynamic binding information, obtained via isothermal titration calorimetry (ITC), provides new insights into the binding of substrates, and of allosteric inhibitor interactions of dihydrodipicolinate synthase (DHDPS) from Escherichia coli. DHDP
Autor:
Sean R. A. Devenish, Renwick C. J. Dobson, Juliet A. Gerrard, Andrew C. Muscroft-Taylor, Belinda B. Guo
Publikováno v:
Biochemical and Biophysical Research Communications. 380:802-806
Dihydrodipicolinate synthase (DHDPS) catalyses the first committed step in the biosynthesis of (S)-lysine, an essential constituent of bacterial cell walls. Escherichia coli DHDPS is homotetrameric, and each monomer contains an N-terminal (alpha/beta
Autor:
Juliet A. Gerrard, F. Grant Pearce, Andrew C. Muscroft-Taylor, Renwick C. J. Dobson, Matthew A. Perugini, Ryan J. Catchpole
Publikováno v:
Archives of biochemistry and biophysics. 503(2)
Escherichia coli dihydrodipicolinate synthase (DHDPS, E.C. 4.2.1.52), a natively homotetrameric enzyme was converted to a monomeric species through the introduction of destabilising interactions at two different subunit interfaces allowing exploratio
Autor:
Renwick C. J. Dobson, Sean R. A. Devenish, Andrew C. Muscroft-Taylor, Juliet A. Gerrard, Tatiana P. Soares da Costa, Geoffrey B. Jameson
Publikováno v:
Biochimie. 92(7)
Dihydrodipicolinate synthase (DHDPS, E.C. 4.2.1.52), a validated antibiotic target, catalyses the first committed step in the lysine biosynthetic pathway: the condensation reaction between (S)-aspartate beta-semialdehyde [(S)-ASA] and pyruvate via th