Zobrazeno 1 - 10
of 90
pro vyhledávání: '"Irwin H. Segel"'
Publikováno v:
Archives of Biochemistry and Biophysics. 489:110-117
The Thiobacillus denitrificans genome contains two sequences corresponding to ATP sulfurylase (Tbd_0210 and Tbd_0874). Both genes were cloned and expressed protein characterized. The larger protein (Tbd_0210; 544 residues) possesses an N-terminal ATP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03679db66094f4997b1a8bc831a1fad0
https://doi.org/10.1016/j.abb.2009.07.026
https://doi.org/10.1016/j.abb.2009.07.026
Publikováno v:
Nature Structural Biology. 9:945-949
The structure of the cooperative hexameric enzyme ATP sulfurylase from Penicillium chrysogenum bound to its allosteric inhibitor, 3'-phosphoadenosine-5'-phosphosulfate (PAPS), was determined to 2.6 A resolution. This structure represents the low subs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44991f1d49b8cc2fa8129a9bd79f46d6
https://doi.org/10.1038/nsb868
https://doi.org/10.1038/nsb868
Ligand-Induced Structural Changes in Adenosine 5‘-Phosphosulfate Kinase from Penicillium chrysogenum
Publikováno v:
Biochemistry. 41:13672-13680
Adenosine 5'-phosphosulfate (APS) kinase catalyzes the second reaction in the two-step, ATP-dependent conversion of inorganic sulfate to 3'-phosphoadenosine 5'-phosphosulfate (PAPS). PAPS serves as the sulfuryl donor for the biosynthesis of all sulfa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24c102e99fb5cb28dc90a40d5fffcc66
https://doi.org/10.1021/bi026556b
https://doi.org/10.1021/bi026556b
Publikováno v:
Archives of Biochemistry and Biophysics. 406:275-288
ATP sulfurylase from the hyperthermophilic chemolithotroph Aquifex aeolicus is a bacterial ortholog of the enzyme from filamentous fungi. (The subunit contains an adenosine 5′-phosphosulfate (APS) kinase-like, C-terminal domain.) The enzyme is high
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b746b1c35c800486d956939fecd5c0a
https://doi.org/10.1016/s0003-9861(02)00428-9
https://doi.org/10.1016/s0003-9861(02)00428-9
Autor:
Douglas C. Nelson, Irwin H. Segel, John D. Beynon, Ian J. MacRae, Sherry L. Huston, Andrew J. Fisher
Publikováno v:
Biochemistry. 40:14509-14517
In sulfur chemolithotrophic bacteria, the enzyme ATP sulfurylase functions to produce ATP and inorganic sulfate from APS and inorganic pyrophosphate, which is the final step in the biological oxidation of hydrogen sulfide to sulfate. The giant tubewo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::913509be9e1bb01591cbd8d670113df9
https://doi.org/10.1021/bi015643l
https://doi.org/10.1021/bi015643l
Publikováno v:
Biochemistry and Molecular Biology Education. 29:3-9
Equations useful for simulating the kinetic behavior of phosphofructokinase are presented. The equations, which are based on the concerted transition (symmetry) model for allosteric enzymes, account for substrate inhibition by MgATP, cooperative bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c20ea30fec84f525e1c39c419c9986b2
https://doi.org/10.1111/j.1539-3429.2001.tb00055.x
https://doi.org/10.1111/j.1539-3429.2001.tb00055.x
Autor:
Irwin H. Segel, Ian J. MacRae
Publikováno v:
Archives of Biochemistry and Biophysics. 361:277-282
Adenosine 5′-phosphosulfate (APS) kinase is subject to strong substrate inhibition by APS. The inhibition has been variously reported to be uncompetitive with respect to MgATP (resulting from the formation of a dead-end E · APS · MgADP complex) o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f02d33c0062ced8a1fb9e09b2c1aa3df
https://doi.org/10.1006/abbi.1998.0993
https://doi.org/10.1006/abbi.1998.0993
Publikováno v:
Journal of Biological Chemistry. 273:28583-28589
The properties of Penicillium chrysogenum adenosine 5′-phosphosulfate (APS) kinase mutated at Ser-107 were examined. Ser-107 is analogous to a serine of the E. coli enzyme that has been shown to serve as an intermediate acceptor in the transfer of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::23c82b2974111b63bd52e3a7d6bb8f8e
https://doi.org/10.1074/jbc.273.44.28583
https://doi.org/10.1074/jbc.273.44.28583
Autor:
Irwin H. Segel, Ian J. MacRae
Publikováno v:
Archives of Biochemistry and Biophysics. 337:17-26
Fungal ATP sulfurylase has been reported to be allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS), the product of adenosine 5'-phosphosulfate (APS) kinase, the second enzyme in the sulfate activation sequence. However, the affin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ad1bc01741ce47c095f9c75ad199013
https://doi.org/10.1006/abbi.1996.9751
https://doi.org/10.1006/abbi.1996.9751
Autor:
Irwin H. Segel
Publikováno v:
Journal of Theoretical Biology. 171:267-280
Chemical and/or radiochemical impurities in a preparation of labeled ligand can introduce artifacts to the analytical Scatchard plot. The causes are either an incorrect assessment of the specific radioactivity of the ligand or an incorrect assessment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::82cfe4cafd1e3a73a409f3c1d79b41db
https://doi.org/10.1006/jtbi.1994.1230
https://doi.org/10.1006/jtbi.1994.1230