Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Susan G. Powers-Lee"'
Publikováno v:
Protein Science. 14:37-44
Carbamoyl phosphate synthetase synchronizes the utilization of two ATP molecules at duplicated ATP-grasp folds to catalyze carbamoyl phosphate formation. To define the dedicated functional role played by each of the two ATP sites, we have carried out
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5e7dfe4121dd77c2b6e8ed9cf253d81
https://doi.org/10.1110/ps.041041305
https://doi.org/10.1110/ps.041041305
Autor:
Susan G. Powers-Lee, Emily J. Hart
Publikováno v:
Protein Science. 17:1120-1128
Evolutionarily conserved triad glutamine amidotransferase (GAT) domains catalyze the cleavage of glutamine to yield ammonia and sequester the ammonia in a tunnel until delivery to a variety of acceptor substrates in synthetase domains of variable str
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https://explore.openaire.eu/search/publication?articleId=doi_dedup___::568aee1c726e19f5afd189487d94ed2e
https://doi.org/10.1110/ps.073428008
https://doi.org/10.1110/ps.073428008
Autor:
Susan G. Powers-Lee, Michael Kothe
Publikováno v:
Protein Science. 13:466-475
Synthesis of carbamoyl phosphate by carbamoyl phosphate synthetase (CPS) requires the coordinated utilization of two molecules of ATP per reaction cycle on duplicated nucleotide-binding sites (N and C). To clarify the contributions of sites N and C t
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https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b60843bce1dc4fc92482a860d3faf62
https://doi.org/10.1110/ps.03416804
https://doi.org/10.1110/ps.03416804
Autor:
Binnur Eroglu, Susan G. Powers-Lee
Publikováno v:
Journal of Biological Chemistry. 277:45466-45472
Although carbamoyl-phosphate synthetases (CPSs) share sequence identity, multidomain structure, and reaction mechanism, they have varying physiological roles and allosteric effectors. Escherichia coli CPS (eCPS) provides CP for both arginine and pyri
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https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8789653187d9fe31acebb1fddfa8fabf
https://doi.org/10.1074/jbc.m208185200
https://doi.org/10.1074/jbc.m208185200
Specificity Determining Residues in Ammonia- and Glutamine-dependent Carbamoyl Phosphate Synthetases
Autor:
Susan G. Powers-Lee, Amna Saeed-Kothe
Publikováno v:
Journal of Biological Chemistry. 277:7231-7238
Carbamoyl phosphate synthetases (CPSs) utilize either glutamine or ammonia for the ATP-dependent generation of carbamoyl phosphate. In glutamine-utilizing CPSs (e.g. the single Escherichia coli CPS and mammalian CPS II), the hydrolysis of glutamine t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ffd9d1e93ac57fa2f70cc41d0fa4582
https://doi.org/10.1074/jbc.m110926200
https://doi.org/10.1074/jbc.m110926200
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1341:35-48
Carbamoyl-phosphate synthetases (CPSases) utilize two molecules of ATP at two homologous domains, B and C, with ATP(B) used to form the enzyme-bound intermediate carboxy-phosphate and ATP(C) used to phosphorylate the carbamate intermediate. To furthe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67374c4cc919f7ec2a87658b0d74c58d
https://doi.org/10.1016/s0167-4838(97)00058-7
https://doi.org/10.1016/s0167-4838(97)00058-7
Autor:
Susan G. Powers-Lee, Angela L. Lim
Publikováno v:
Archives of Biochemistry and Biophysics. 339:344-352
Carbamoyl-phosphate synthetases (CPSases) bind two molecules of ATP at two internally duplicated domains. Previous affinity labeling studies with the ATP analog 5′-p-fluorosulfonylbenzoyladenosine (FSBA; Kim, H., Kelly, R. E., and Evans, D. R. (199
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https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ecfa6ef0c05cf741e87344d7b87c406
https://doi.org/10.1006/abbi.1997.9887
https://doi.org/10.1006/abbi.1997.9887
Autor:
Susan G. Powers-Lee, M D Potter
Publikováno v:
Journal of Biological Chemistry. 267:2023-2031
The gamma-phosphate subsites of the MgATP sites of rat liver carbamoyl-phosphate synthetase I have been defined by use of the ATP analog 5'-p-fluorosulfonylbenzoyladenosine (FSBA). The synthetase utilizes two molecules of MgATP, apparently in mechani
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https://explore.openaire.eu/search/publication?articleId=doi_________::9e77f23a5674db4b2b5473367c29b201
https://doi.org/10.1016/s0021-9258(18)46048-6
https://doi.org/10.1016/s0021-9258(18)46048-6
Autor:
Susan G. Powers-Lee, Emily J. Hart
Human carbamoyl phosphate synthetase (hCPS) has evolved critical features that allow it to remove excess and potentially neurotoxic ammonia via the urea cycle, including use of only free ammonia as a nitrogen donor, a Km for ammonia 100-fold lower th
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https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67d5034b5888d28ef11adbea59d28843
https://europepmc.org/articles/PMC2645840/
https://europepmc.org/articles/PMC2645840/
Autor:
Mary-ann Brandt, Susan G. Powers-Lee
Publikováno v:
Archives of Biochemistry and Biophysics. 290:14-20
A selective interaction of rat liver carbamoyl phosphate synthetase I with cardiolipin, and other anionic phospholipids, has been demonstrated. The enzymatic activity of the synthetase is inhibited by cardiolipin and, to a lesser extent, by phosphati
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https://doi.org/10.1016/0003-9861(91)90585-7
https://doi.org/10.1016/0003-9861(91)90585-7