Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Audrey L. Lamb"'
Autor:
Nikola Kenjić, Kathleen M. Meneely, Daniel J. Wherritt, Melissa C. Denler, Timothy A. Jackson, Graham R. Moran, Audrey L. Lamb
Publikováno v:
Journal of the American Chemical Society. 144:12769-12780
RibB (3,4-dihydroxy-2-butanone 4-phosphate synthase) is a magnesium-dependent enzyme that excises the C4 of d-ribulose-5-phosphate (d-Ru5P) as formate. RibB generates the four-carbon substrate for lumazine synthase that is incorporated into the xylen
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:
Madison M. Smith, Dariush C. Fourozesh, Audrey L. Lamb, Kathleen M. Meneely, Graham R. Moran, Brett A. Beaupre
Publikováno v:
Biochemistry. 60:3027-3039
Guanosine triphosphate (GTP) cyclohydrolase II (RibA) is one of three enzymes that hydrolytically cleave the C8-N9 bond of the GTP guanine. RibA also catalyzes a subsequent hydrolytic attack at the base liberating formate and in addition cleaves the
Publikováno v:
Biochemistry
Cysteine dioxygenase (CDO) structurally resembles cupin enzymes that use a 3-His/1-Glu coordination scheme. However, the glutamate ligand is substituted with a cysteine (Cys93) residue, which forms a thioether bond with tyrosine (Tyr157) under physio
Autor:
Pierce T. ONeil, Katheryn Vela, Braelyn M. Page, Jeffrey S. McFarlane, Collette L. Wright, Kathleen M. Meneely, Aron W. Fenton, Audrey L. Lamb, Liskin Swint-Kruse
Publikováno v:
Biophysical Journal. 122:475a
Autor:
Tiffany Wu, Kathleen M. Meneely, Kathryn D. Fenton, Liskin Swint-Kruse, Aron W. Fenton, Audrey L. Lamb, Tyler A. Martin
Publikováno v:
Protein Sci
Some protein positions play special roles in determining the magnitude of protein function: at such “rheostat” positions, varied amino acid substitutions give rise to a continuum of functional outcomes, from wild type (or enhanced), to intermedia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c6b6f244ff4b43ec6e1b62d5fd7a76b
https://europepmc.org/articles/PMC8819835/
https://europepmc.org/articles/PMC8819835/
Autor:
Madison M, Smith, Brett A, Beaupre, Dariush C, Fourozesh, Kathleen M, Meneely, Audrey L, Lamb, Graham R, Moran
Publikováno v:
Biochemistry. 60(40)
Guanosine triphosphate (GTP) cyclohydrolase II (RibA) is one of three enzymes that hydrolytically cleave the C8-N9 bond of the GTP guanine. RibA also catalyzes a subsequent hydrolytic attack at the base liberating formate and in addition cleaves the
Autor:
Jeffrey S. McFarlane, Jian Zhang, Sanshan Wang, Xiaoguang Lei, Audrey L. Lamb, Graham R. Moran
Publikováno v:
J Biol Chem
Pseudopaline and staphylopine are opine metallophores biosynthesized by Pseudomonas aeruginosa and Staphylococcus aureus, respectively. The final step in opine metallophore biosynthesis is the condensation of the product of a nicotianamine (NA) synth
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