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.
| Original language | English |
|---|---|
| Pages (from-to) | 4239-4245 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 250 |
| Issue number | 11 |
| State | Published - 1975 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry
Cite this
The hepatic adenylate cyclase system. I. Evidence for transition states and structural requirements for guanine nucleotide activation. / Salomon, Y.; Lin, M. C.; Londos, C.; Rendell, M.; Rodbell, M.
In: Journal of Biological Chemistry, Vol. 250, No. 11, 1975, p. 4239-4245.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The hepatic adenylate cyclase system. I. Evidence for transition states and structural requirements for guanine nucleotide activation
AU - Salomon, Y.
AU - Lin, M. C.
AU - Londos, C.
AU - Rendell, M.
AU - Rodbell, M.
PY - 1975
Y1 - 1975
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0016812088&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0016812088&partnerID=8YFLogxK
M3 - Article
C2 - 1126949
AN - SCOPUS:0016812088
VL - 250
SP - 4239
EP - 4245
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 11
ER -