Zobrazeno 1 - 10
of 128
pro vyhledávání: '"Lukasz Lebioda"'
Publikováno v:
Archives of Biochemistry and Biophysics. 545:108-115
Sea worm, Amphitrite ornata, has evolved its globin (an O(2) carrier) also to serves as a dehaloperoxidase (DHP) to detoxify haloaromatic pollutants generated by competing species. A previous mutagenesis study by our groups on both DHP and sperm whal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b9c6642bda224662ccaf2b39ccb266d
https://doi.org/10.1016/j.abb.2014.01.010
https://doi.org/10.1016/j.abb.2014.01.010
Publikováno v:
Biochemistry. 52:6203-6210
The hemoglobin of sea worm Amphitrite ornata, which for historical reasons is abbreviated as DHP for dehaloperoxidase, has two physiological functions: it binds dioxygen in the ferrous state and dehalogenates halophenols, such as 2,4,6-trichloropheno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a4e647980df2a76e6885e683e09f522
https://doi.org/10.1021/bi400627w
https://doi.org/10.1021/bi400627w
Autor:
Leslie L. Lovelace, Shengfang Sun, Lukasz Lebioda, Lesa R. Celeste, Chunxue Wang, John H. Dawson, Xiao Huang
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68:1465-1471
Sperm whale myoglobin (Mb) has weak dehaloperoxidase activity and catalyzes the peroxidative dehalogenation of 2,4,6-trichlorophenol (TCP) to 2,6-dichloroquinone. Crystals of Mb and of its more active G65T variant were used to study the binding of TC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca479643f12edd1c617ac7160d4034d7
https://doi.org/10.1107/s1744309112045514
https://doi.org/10.1107/s1744309112045514
Publikováno v:
Journal of Inorganic Biochemistry. 111:187-194
In the presence of magnesium, enolase catalyzes the dehydration of 2-phospho-D-glycerate (PGA) to phosphoenolpyruvate (PEP) in glycolysis and the reverse reaction in gluconeogensis at comparable rates. The structure of human neuron specific enolase (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b976c02165524d6e64808c3ffb9a1fea
https://doi.org/10.1016/j.jinorgbio.2012.02.011
https://doi.org/10.1016/j.jinorgbio.2012.02.011
Autor:
Magdalena Bielak, Geqing Chai, Wladek Minor, Lesa R. Celeste, Lukasz Lebioda, Leslie L. Lovelace
Publikováno v:
Protein Science. 21:219-228
N(10) -formyltetrahydrofolate synthetase (FTHFS) is a folate enzyme that catalyzes the formylation of tetrahydrofolate (THF) in an ATP dependent manner. Structures of FTHFS from the thermophilic homoacetogen, Moorella thermoacetica, complexed with (1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80a62fc60dad65902c5457a0dc6a3ddd
https://doi.org/10.1002/pro.2005
https://doi.org/10.1002/pro.2005
Publikováno v:
Journal of Biological Chemistry. 286:17585-17592
C8 is one of five complement proteins that assemble on bacterial membranes to form the lethal pore-like “membrane attack complex” (MAC) of complement. The MAC consists of one C5b, C6, C7, and C8 and 12–18 molecules of C9. C8 is composed of thre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b38224c399849a479fd871f69a23841
https://doi.org/10.1074/jbc.m111.219766
https://doi.org/10.1074/jbc.m111.219766
Publikováno v:
Journal of Molecular Evolution. 72:306-314
Crystal structures of human thymidylate synthase (hTS) revealed that the protein exists in active and inactive conformations, defined by the position of a loop containing the active site nucleophile. TS is highly homologous among diverse species; how
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e68318277cd5410cb24c6ce33c1c9326
https://doi.org/10.1007/s00239-011-9433-8
https://doi.org/10.1007/s00239-011-9433-8
Autor:
BeiBei Luo, Al-Motassem Yousef, Jayanthi Repalli, Lukasz Lebioda, Saphronia R. Johnson, Sondra H. Berger
Publikováno v:
Protein Science. 20:87-94
Thymidylate synthase (TS) is a well-validated cancer target that undergoes conformational switching between active and inactive states. Two mutant human TS (hTS) proteins are predicted from crystal structures to be stabilized in an inactive conformat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c944583bb497c88512a0cd312018a5c0
https://doi.org/10.1002/pro.539
https://doi.org/10.1002/pro.539
Autor:
Brian Knuckley, Paul R. Thompson, Corey P. Causey, Leslie L. Lovelace, Lukasz Lebioda, Justin E. Jones, Heather Flick
Publikováno v:
Bioorganic Chemistry. 38:62-73
Helicobacter pylori encodes a potential virulence factor, agmatine deiminase (HpAgD), which catalyzes the conversion of agmatine to N-carbamoyl putrescine (NCP) and ammonia - agmatine is decarboxylated arginine. Agmatine is an endogenous human cell s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::863c943590a1fdf41016809a367eee91
https://doi.org/10.1016/j.bioorg.2009.11.004
https://doi.org/10.1016/j.bioorg.2009.11.004
Autor:
Lydia M. Gibson, Saphronia R. Johnson, Lukasz Lebioda, Leslie L. Lovelace, Sondra H. Berger, Brittnaie J. Bell
Publikováno v:
Protein Science. 18:1628-1636
Loop 181-197 of human thymidylate synthase (hTS) populates two major conformations, essentially corresponding to the loop flipped by 180 degrees . In one of the conformations, the catalytic Cys195 residue lies distant from the active site making the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00cdcd6b48dafdfa6d68533008c92737
https://doi.org/10.1002/pro.171
https://doi.org/10.1002/pro.171