Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Trey A Ronnebaum"'
Publikováno v:
Biochemistry. 61(18)
The regiospecific prenylation of an aromatic amino acid catalyzed by a dimethylallyl-l-tryptophan synthase (DMATS) is a key step in the biosynthesis of many fungal and bacterial natural products. DMATS enzymes share a common "ABBA" fold with divergen
Publikováno v:
Biochemistry. 61:2025-2035
Autor:
Catherine L. Shelton, Kathleen M. Meneely, Trey A. Ronnebaum, Annemarie S. Chilton, Andrew P. Riley, Thomas E. Prisinzano, Audrey L. Lamb
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 27:541-551
Pseudomonas aeruginosa is an increasingly antibiotic-resistant pathogen that causes severe lung infections, burn wound infections, and diabetic foot infections. P. aeruginosa produces the siderophore pyochelin through the use of a non-ribosomal pepti
Autor:
Alex A. Meier, Hee-Jung Moon, Sinan Sabuncu, Priya Singh, Trey A. Ronnebaum, Siyu Ou, Justin T. Douglas, Timothy A. Jackson, Pierre Moënne-Loccoz, Minae Mure
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 22; Pages: 13966
Lysyl oxidase-2 (LOXL2) is a Cu2+ and lysine tyrosylquinone (LTQ)-dependent amine oxidase that catalyzes the oxidative deamination of peptidyl lysine and hydroxylysine residues to promote crosslinking of extracellular matrix proteins. LTQ is post-tra
Autor:
Alex A, Meier, Hee-Jung, Moon, Sinan, Sabuncu, Priya, Singh, Trey A, Ronnebaum, Siyu, Ou, Justin T, Douglas, Timothy A, Jackson, Pierre, Moënne-Loccoz, Minae, Mure
Publikováno v:
International journal of molecular sciences. 23(22)
Lysyl oxidase-2 (LOXL2) is a Cu
Publikováno v:
Biochemistry. 59:4744-4754
The sesquiterpene cyclase epi-isozizaene synthase (EIZS) catalyzes the cyclization of farnesyl diphosphate to form the tricyclic precursor of the antibiotic albaflavenone. The hydrophobic active site is largely defined by aromatic residues that direc
Autor:
Trey A. Ronnebaum, Samuel A. Eaton, Emily A. E. Brackhahn, Jacque L. Faylo, Kushol Gupta, David W. Christianson
Publikováno v:
The FASEB Journal. 36
Publikováno v:
Acc Chem Res
ConspectusThe magnificent chemodiversity of more than 95 000 terpenoid natural products identified to date largely originates from catalysis by two types of terpene synthases, prenyltransferases and cyclases. Prenyltransferases utilize 5-carbon build
Autor:
Jeffrey S. McFarlane, Annemarie S. Chilton, Kathleen M. Meneely, Aron W. Fenton, Audrey L. Lamb, Trey A Ronnebaum
Publikováno v:
Acta Crystallogr F Struct Biol Commun
Human liver pyruvate kinase (hLPYK) converts phosphoenolpyruvate to pyruvate in the final step of glycolysis. hLPYK is allosterically activated by fructose-1,6-bisphosphate (Fru-1,6-BP). The allosteric site, as defined by previous structural studies,
Autor:
Trey A Ronnebaum, Audrey L. Lamb, Thomas E. Prisinzano, Squire J. Booker, Jeffrey S. McFarlane
Publikováno v:
Biochemistry. 58:665-678
Nonribosomal peptide synthetases use tailoring domains to incorporate chemical diversity into the final natural product. A structurally unique set of tailoring domains are found to be stuffed within adenylation domains and have only recently begun to