File Download
Links for fulltext
(May Require Subscription)
- Scopus: eid_2-s2.0-0016812088
- PMID: 1126949
- WOS: WOS:A1975AE57800029
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: The hepatic adenylate cyclase system. I. Evidence for transition states and structural requirements for guanine nucleotide activation
Title | The hepatic adenylate cyclase system. I. Evidence for transition states and structural requirements for guanine nucleotide activation |
---|---|
Authors | |
Issue Date | 1975 |
Publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ |
Citation | Journal Of Biological Chemistry, 1975, v. 250 n. 11, p. 4239-4245 How to Cite? |
Abstract | Previous studies showed that guanine nucleotides, acting at a site termed the nucleotide regulatory site, are required for activation of hepatic adenylate cyclase, and that glucagon facilitates this process. This study shows that only guanine nucleotides containing triphosphate groups at the 5' position of ribose (or 3' deoxyribose) are capable of activating the enzyme. The terminal phosphate is not utilized in the activation process, since 5' guanylylimidodiphosphate [Gpp(NH)p] and 5' guanylyl methylenediphosphonate, analogues of guanosine triphosphate that are not utilized in transferase or hydrolase reactions, stimulate enzyme activity. The nucleotides bind in their free form at the regulatory site; chelation by magnesium ion shifts the apparent concentration dependence for activation by Gpp(NH)p. Guanosine diphosphate inhibits competitively Gpp(NH)p stimulated activity and inhibits basal activity and activities stimulated by glucagon. |
Persistent Identifier | http://hdl.handle.net/10722/167436 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Salomon, Y | en_US |
dc.contributor.author | Lin, MC | en_US |
dc.contributor.author | Londos, C | en_US |
dc.date.accessioned | 2012-10-08T03:06:58Z | - |
dc.date.available | 2012-10-08T03:06:58Z | - |
dc.date.issued | 1975 | en_US |
dc.identifier.citation | Journal Of Biological Chemistry, 1975, v. 250 n. 11, p. 4239-4245 | en_US |
dc.identifier.issn | 0021-9258 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/167436 | - |
dc.description.abstract | Previous studies showed that guanine nucleotides, acting at a site termed the nucleotide regulatory site, are required for activation of hepatic adenylate cyclase, and that glucagon facilitates this process. This study shows that only guanine nucleotides containing triphosphate groups at the 5' position of ribose (or 3' deoxyribose) are capable of activating the enzyme. The terminal phosphate is not utilized in the activation process, since 5' guanylylimidodiphosphate [Gpp(NH)p] and 5' guanylyl methylenediphosphonate, analogues of guanosine triphosphate that are not utilized in transferase or hydrolase reactions, stimulate enzyme activity. The nucleotides bind in their free form at the regulatory site; chelation by magnesium ion shifts the apparent concentration dependence for activation by Gpp(NH)p. Guanosine diphosphate inhibits competitively Gpp(NH)p stimulated activity and inhibits basal activity and activities stimulated by glucagon. | en_US |
dc.language | eng | en_US |
dc.publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ | en_US |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.subject.mesh | Adenylate Cyclase - Metabolism | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Binding, Competitive | en_US |
dc.subject.mesh | Cell Membrane - Drug Effects - Enzymology | en_US |
dc.subject.mesh | Enzyme Activation - Drug Effects | en_US |
dc.subject.mesh | Glucagon - Pharmacology | en_US |
dc.subject.mesh | Guanine Nucleotides - Pharmacology | en_US |
dc.subject.mesh | Guanosine Triphosphate - Pharmacology | en_US |
dc.subject.mesh | Kinetics | en_US |
dc.subject.mesh | Liver - Drug Effects - Enzymology | en_US |
dc.subject.mesh | Magnesium - Pharmacology | en_US |
dc.subject.mesh | Protein Binding | en_US |
dc.subject.mesh | Rats | en_US |
dc.subject.mesh | Structure-Activity Relationship | en_US |
dc.subject.mesh | Time Factors | en_US |
dc.title | The hepatic adenylate cyclase system. I. Evidence for transition states and structural requirements for guanine nucleotide activation | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lin, MC:mcllin@hkucc.hku.hk | en_US |
dc.identifier.authority | Lin, MC=rp00746 | en_US |
dc.description.nature | link_to_OA_fulltext | en_US |
dc.identifier.pmid | 1126949 | - |
dc.identifier.scopus | eid_2-s2.0-0016812088 | en_US |
dc.identifier.volume | 250 | en_US |
dc.identifier.issue | 11 | en_US |
dc.identifier.spage | 4239 | en_US |
dc.identifier.epage | 4245 | en_US |
dc.identifier.isi | WOS:A1975AE57800029 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Salomon, Y=7006956498 | en_US |
dc.identifier.scopusauthorid | Lin, MC=7404816359 | en_US |
dc.identifier.scopusauthorid | Londos, C=7005200523 | en_US |
dc.identifier.issnl | 0021-9258 | - |