Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Grit Daniela Straganz"'
Publikováno v:
Lin, Y, Stańczak, A, Manchev, Y, Straganz, G & De Visser, S 2019, ' Can a mononuclear iron(III)-superoxo active site catalyze the decarboxylation of dodecanoic acid in UndA to produce biofuels? ', Chemistry – A European Journal . https://doi.org/10.1002/chem.201903783
Decarboxylation of fatty acids is an important reaction in cell metabolism, but also has potential in biotechnology for the biosynthesis of hydrocarbons as biofuels. The recently discovered nonheme iron decarboxylase UndA is involved in the biosynthe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6cd3ad718a0c5955ec5a387d81887a3
https://pure.manchester.ac.uk/ws/files/137019896/Agnieszka_nonheme_paper_v8.pdf
https://pure.manchester.ac.uk/ws/files/137019896/Agnieszka_nonheme_paper_v8.pdf
Publikováno v:
Frontiers in Chemistry
Timmins, A, Fowler, N, Warwicker, J, Straganz, G D & De Visser, S 2018, ' Does substrate positioning affect the selectivity and reactivity in the hectochlorin biosynthesis halogenase? ', Frontiers in Chemistry, vol. 6, no. 513 . https://doi.org/10.3389/fchem.2018.00513
Frontiers in Chemistry, Vol 6 (2018)
Timmins, A, Fowler, N, Warwicker, J, Straganz, G D & De Visser, S 2018, ' Does substrate positioning affect the selectivity and reactivity in the hectochlorin biosynthesis halogenase? ', Frontiers in Chemistry, vol. 6, no. 513 . https://doi.org/10.3389/fchem.2018.00513
Frontiers in Chemistry, Vol 6 (2018)
In this work we present the first computational study on the hectochlorin biosynthesis enzyme HctB, which is a unique three-domain halogenase that activates non-amino acid moieties tethered to an acyl-carrier, and as such may have biotechnological re
Autor:
Cristiana Maria Loredana Di Giuro, Devesh Kumar, Grit Daniela Straganz, Cornelia Konstantinovics, Gideon Grogan, Sarah Pratter, Sam P. de Visser, Erich Leitner
Publikováno v:
Angewandte Chemie International Edition. 52:9677-9681
The ol' switcheroo: The enantioselectivity of an O2-dependent hydroxylation at a mononuclear non-heme iron center was switched from S to R by changing the geometry of the substrate ligand at the metal center through protein redesign. This rational ap
Autor:
Geneviève Morrow, Robert M. Tanguay, Pidder Jansen-Dürr, Haymo Pircher, Daniela Ehehalt, Grit Daniela Straganz
Publikováno v:
The Journal of Biological Chemistry
Background: Human FAHD1 is a member of the FAH enzyme superfamily with unknown enzymatic activity. Results: FAHD1 exhibits acylpyruvase activity, demonstrated by the hydrolysis of acetylpyruvate and fumarylpyruvate in vitro. Conclusion: We identified
Autor:
Michael L. Neidig, Grit Daniela Straganz, Graham R. Moran, Edward I. Solomon, Adrienne R. Diebold
Publikováno v:
Biochemistry. 49:6945-6952
The oxygen activating mononuclear non-heme ferrous enzymes catalyze a diverse range of chemistry yet typically maintain a common structural motif: two histidines and a carboxylate coordinating the iron center in a facial triad. A new FeII coordinatin
Publikováno v:
FEBS Journal. 276:5983-5997
Cupins constitute a large and widespread superfamily of beta-barrel proteins in which a mononuclear metal site is both a conserved feature of the structure and a source of functional diversity. Metal-binding residues are contributed from two core mot
Publikováno v:
Biochemical Journal. 418:403-411
beta-diketone-cleaving enzyme Dke1 is a homotetrameric Fe2+-dependent dioxygenase from Acinetobacter johnsonii. The Dke1protomer adopts a single-domain beta-barrel fold characteristic of the cupin superfamily of proteins and features a mononuclear no
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 42:85-89
Saturation–transfer–difference NMR spectroscopy (STD NMR) is used to delineate noncovalent enzyme–substrate interactions of β-glycosidases from Pyrococcus furiosus and Aspergillus fumigatus under binding-only conditions at low temperatures, an
Autor:
Bernd Nidetzky, Grit Daniela Straganz
Publikováno v:
ChemBioChem. 7:1536-1548
A facial triad of two histidine side chains and one aspartate or glutamate side chain forms the canonical metal-coordinating motif in the catalytic centers of various mononuclear non-heme Fe(II) enzymes. Although these active sites are based on total
Publikováno v:
Journal of molecular catalysis. B, Enzymatic
39 (2006): 171–178. doi:10.1016/j.molcatb.2006.01.019
info:cnr-pdr/source/autori:Straganz G.D., Egger S., Aquino G., D'Auria S., Nidetzky B./titolo:Exploring the cupin-type metal-coordinating signature of acetylacetone dioxygenase Dke1 with site-directed mutagenesis: catalytic reaction profile and Fe2+ binding stability of Glu-69->Gln mutant./doi:10.1016%2Fj.molcatb.2006.01.019/rivista:Journal of molecular catalysis. B, Enzymatic (Print)/anno:2006/pagina_da:171/pagina_a:178/intervallo_pagine:171–178/volume:39
39 (2006): 171–178. doi:10.1016/j.molcatb.2006.01.019
info:cnr-pdr/source/autori:Straganz G.D., Egger S., Aquino G., D'Auria S., Nidetzky B./titolo:Exploring the cupin-type metal-coordinating signature of acetylacetone dioxygenase Dke1 with site-directed mutagenesis: catalytic reaction profile and Fe2+ binding stability of Glu-69->Gln mutant./doi:10.1016%2Fj.molcatb.2006.01.019/rivista:Journal of molecular catalysis. B, Enzymatic (Print)/anno:2006/pagina_da:171/pagina_a:178/intervallo_pagine:171–178/volume:39
Glu-69 belongs to a proposed active-site consensus motif His 62 -X-His 64 -X 4 -Glu 69 (where X is any amino acid) that acetylacetone dioxygenase Dke1 from Acinetobacter johnsonii shares with structurally related non-heme metal enzymes of the cupin p