Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Benjamin R. Burgess"'
Autor:
Lauren M. Angley, Michael D. W. Griffin, Renwick C. J. Dobson, Andrew J. Watson, Rachel A. North, Antony J. Fairbanks, André O. Hudson, Sarah C. Atkinson, Benjamin R. Burgess, Hironori Suzuki, Sarah A. Kessans, Arvind Varsani
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69:306-312
The enzyme N-acetylneuraminate lyase (EC 4.1.3.3) is involved in the metabolism of sialic acids. Specifically, the enzyme catalyzes the retro-aldol cleavage of N-acetylneuraminic acid to form N-acetyl-D-mannosamine and pyruvate. Sialic acids comprise
Autor:
F. Grant Pearce, Matthew A. Perugini, Renwick C. J. Dobson, Craig A. Hutton, Juliet A. Gerrard, Benjamin R. Burgess, Sean R. A. Devenish, Genevieve L. Evans, Voula Mitsakos
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 18:842-844
Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis and an important antibiotic target. The specificity of a range of heterocyclic product analogues against DHDPS from three pathogenic species, Bacillus anthracis, Mycobacteriu
Autor:
Matthew A. Perugini, Benjamin R. Burgess, Renwick C. J. Dobson, Geoffrey B. Jameson, Con Dogovski, Michael W. Parker
In recent years, dihydrodipicolinate synthase (DHDPS; EC 4.2.1.52) has received considerable attention from both mechanistic and structural viewpoints. DHDPS is part of the diaminopimelate pathway leading to lysine, coupling (S)-aspartate-beta-semial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c18c687b360b3d1885df0912fc6af23
https://europepmc.org/articles/PMC2443978/
https://europepmc.org/articles/PMC2443978/