Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Penelope J Cross"'
Publikováno v:
PLoS ONE, Vol 11, Iss 2, p e0145187 (2016)
Neisseria meningitidis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (NmeDAH7PS) adopts a homotetrameric structure consisting of an extensive and a less extensive interface. Perturbation of the less extensive interface through a single mutatio
Externí odkaz:
https://doaj.org/article/c30d4367f5ec4c1981ed0c3adb2ff44e
Autor:
Anutthaman Parthasarathy, Penelope J. Cross, Renwick C. J. Dobson, Lily E. Adams, Michael A. Savka, André O. Hudson
Publikováno v:
Frontiers in Molecular Biosciences, Vol 5 (2018)
Tyrosine, phenylalanine and tryptophan are the three aromatic amino acids (AAA) involved in protein synthesis. These amino acids and their metabolism are linked to the synthesis of a variety of secondary metabolites, a subset of which are involved in
Externí odkaz:
https://doaj.org/article/afa7c0b23b374e4ca09d868ce7998ef0
Autor:
Mary M. Leeman, Michael R. Oliver, Rachel A. North, Austin J. Bartl, Müge Kasanmascheff, Renwick C. J. Dobson, Hironori Suzuki, Michael D. W. Griffin, Katherine A. Donovan, André O. Hudson, Jennifer M. Crowther, Penelope J. Cross
Publikováno v:
Crowther, J M, Cross, P J, Oliver, M R, Leeman, M M, Bartl, A J, Weatherhead, A W, North, R A, Donovan, K A, Griffin, M D W, Suzuki, H, Hudson, A O, Kasanmascheff, M & Dobson, R C J 2019, ' Structure–function analyses of two plant meso-diaminopimelate decarboxylase isoforms reveal that active-site gating provides stereochemical control ', Journal of Biological Chemistry, vol. 294, no. 21, pp. 8505-8515 . https://doi.org/10.1074/jbc.RA118.006825
J Biol Chem
J Biol Chem
meso-Diaminopimelate decarboxylase catalyzes the decarboxylation of meso-diaminopimelate, the final reaction in the diaminopimelate l-lysine biosynthetic pathway. It is the only known pyridoxal-5-phosphate–dependent decarboxylase that catalyzes the
Publikováno v:
Proceedings of the National Academy of Sciences. 115:3006-3011
Most proteins comprise two or more domains from a limited suite of protein families. These domains are often rearranged in various combinations through gene fusion events to evolve new protein functions, including the acquisition of protein allostery
Autor:
Renwick C. J. Dobson, Lily E. Adams, Penelope J. Cross, André O. Hudson, Michael A. Savka, Anutthaman Parthasarathy
Publikováno v:
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences, Vol 5 (2018)
Frontiers in Molecular Biosciences, Vol 5 (2018)
Tyrosine, phenylalanine and tryptophan are the three aromatic amino acids (AAA) involved in protein synthesis. These amino acids and their metabolism are linked to the synthesis of a variety of secondary metabolites, a subset of which are involved in
Publikováno v:
Current Opinion in Structural Biology. 29:102-111
Allosteric regulation of enzyme activity plays important metabolic roles. Here we review the allostery of enzymes of amino-acid metabolism conferred by a discrete domain known as the ACT domain. This domain of 60-70 residues has a βαββαβ topolo
Autor:
Timothy M. Allison, Amy L. Pietersma, Fiona C. Cochrane, Sarah M. Wilson-Coutts, Penelope J. Cross, Emily J. Parker
Publikováno v:
Protein Science. 22:1087-1099
Neisseria meningitidis is the causative agent of meningitis and meningococcal septicemia is a major cause of disease worldwide, resulting in brain damage and hearing loss, and can be fatal in a large proportion of cases. The enzyme 3-deoxy-d-arabino-
Autor:
Geoffrey B. Jameson, Timothy M. Allison, Emily J. Parker, Penelope J. Cross, Renwick C. J. Dobson
Publikováno v:
Proceedings of the National Academy of Sciences. 110:2111-2116
Allosteric regulation of protein function is a critical component of metabolic control. Its importance is underpinned by the diversity of mechanisms and its presence in all three domains of life. The first enzyme of the aromatic amino acid biosynthes
Autor:
Emilia C. Arturo, Linda Stith, Annie Heroux, Emily J. Parker, Eileen K. Jaffe, Kushol Gupta, Patrick J. Loll, Penelope J. Cross
Improved understanding of the relationship among structure, dynamics, and function for the enzyme phenylalanine hydroxylase (PAH) can lead to needed new therapies for phenylketonuria, the most common inborn error of amino acid metabolism. PAH is a mu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b76b072d0a554d3c0961e918b4f58c1b
https://europepmc.org/articles/PMC4780608/
https://europepmc.org/articles/PMC4780608/
Dynamic Cross-Talk among Remote Binding Sites: The Molecular Basis for Unusual Synergistic Allostery
Publikováno v:
Journal of Molecular Biology. 415:716-726
Allosteric regulation of protein function is critical for metabolic control. Binding of allosteric effectors elicits a functional change in a remote ligand binding site on a protein by altering the equilibrium between different forms in the protein e