Zobrazeno 1 - 10 of 25 pro vyhledávání: '"I H, Segel"'
1
Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues
Autor: I J, MacRae, A B, Rose, I H, Segel
Publikováno v: The Journal of biological chemistry. 273(44)
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 a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f568d29a7bccc23e9a7ecbe7e113e79b
https://pubmed.ncbi.nlm.nih.gov/9786849
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2
Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum. Identification of a likely allosteric domain
Autor: B A, Foster, S M, Thomas, J A, Mahr, F, Renosto, H C, Patel, I H, Segel
Publikováno v: The Journal of biological chemistry. 269(31)
Fungal (Penicillium chrysogenum) and yeast (Saccharomyces cerevisiae) ATP sulfurylases were shown to have very similar kinetic and chemical properties except that the fungal enzyme (a) contains a highly reactive Cys residue (SH-1) whose modification
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::43e1d3220200897e8929c21355c81927
https://pubmed.ncbi.nlm.nih.gov/8051058
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3
Regulation of inorganic sulfate activation in filamentous fungi. Allosteric inhibition of ATP sulfurylase by 3'-phosphoadenosine-5'-phosphosulfate
Autor: F, Renosto, R L, Martin, L M, Wailes, L A, Daley, I H, Segel
Publikováno v: The Journal of biological chemistry. 265(18)
ATP sulfurylases from Penicillium chrysogenum, Penicillium duponti, Aspergillus nidulans, and Neurospora crassa are strongly inhibited by 3'-phosphoadenosine-5'-phosphosulfate (PAPS), the product of the second (adenosine-5'-phosphosulfate kinase-cata
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4eaf03fd47fc792e5c8900c020a9e2f9
https://pubmed.ncbi.nlm.nih.gov/2162344
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4
Interaction of cyclic adenosine 3':5'-monophosphate with protein kinase. Equilibrium binding models
Autor: I H Segel, J R Ogez
Publikováno v: Journal of Biological Chemistry. 251:4551-4556
A number of potential models for the interaction of cyclic AMP with protein kinase (RC or R2C2) have been examined. These include: Model 1, the simultaneous binding of cyclic AMP and release of C (catalytic subunit) from an independent RC protomer; M
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8c9c47f8810fddae99ea78a5aee580f5
https://doi.org/10.1016/s0021-9258(17)33237-4
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6
Glycogen phosphorylase from Neurospora crassa: purification of a high-specific-activity, non-phosphorylated form
Autor: J Cuppoletti, I H Segel
A highly active glycogen phosphorylase was purified from Neurospora crassa by polyethylene glycol fractionation at pH 6.16 combined with standard techniques (chromatography and salt fractionation). The final preparation had a specific activity of 65
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6da7d66c11748db5b77ce31e3e2f9946
https://europepmc.org/articles/PMC216884/
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8
ATP sulfurylase from Penicillium chrysogenum. Molecular basis of the sigmoidal velocity curves induced by sulfhydryl group modification
Autor: F, Renosto, R L, Martin, I H, Segel
Publikováno v: The Journal of biological chemistry. 262(34)
ATP sulfurylase from Penicillium chrysogenum is a noncooperative homooligomer containing three free sulfhydryl groups per subunit. Under nondenaturing conditions, one SH group per subunit was modified by 5,5'-dithiobis-(2-nitrobenzoate), or N-ethylma
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6158e633c77693eee935ee00d7c4dee4
https://pubmed.ncbi.nlm.nih.gov/2824486
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9
Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. Determining ligand dissociation constants of binary and ternary complexes from the kinetics of enzyme inactivation
Autor: F, Renosto, P A, Seubert, P, Knudson, I H, Segel
Publikováno v: The Journal of biological chemistry. 260(22)
Adenosine 5-phosphosulfate (APS) kinase from Penicillium chrysogenum is irreversibly inactivated by trinitrobenzene sulfonate in a pseudo-first order process. Under standard assay conditions kapp was 1.9 X 10(-3) s-1. Saturating MgATP or MgADP decrea
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e53a373fbe690859a5e3dfb9cbdea1fa
https://pubmed.ncbi.nlm.nih.gov/2995351
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10
ATP sulfurylase from Penicillium chrysogenum: measurements of the true specific activity of an enzyme subject to potent product inhibition and a reassessment of the kinetic mechanism
Autor: P A, Seubert, L, Hoang, F, Renosto, I H, Segel
Publikováno v: Archives of biochemistry and biophysics. 225(2)
Homogeneous ATP sulfurylase from Penicillium chrysogenum has been reported to have an extremely low activity toward its physiological inorganic substrate, sulfate. This low activity is an artifact resulting from potent product inhibition by 5'-adenyl
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::228b25b364caae2a5cdb958493942d65
https://pubmed.ncbi.nlm.nih.gov/6312889
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