Abstract
The interaction of Mg2+, AMP, and fructose 2,6-bisphosphate with respect to rabbit liver fructose-1,6-bisphosphatase was investigated by studying initial-rate kinetics of the system at pH 9.5. A rapid-equilibrium Random Bi Bi mechanism is suggested for the rabbit liver enzyme from the kinetic data. Our kinetic findings indicate that Mg2+ and the inhibitor AMP are mutually exclusive in their binding to fructose-1,6-bisphosphatase. This probably is the mechanism for AMP regulation of fructose-1,6-bisphosphatase and thus, to some extent, gluconeogenesis. A kinetic model for the interaction of these ligands with respect to rabbit liver fructose-1,6-bisphosphatase is presented.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 7401-7406 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 265 |
| Issue number | 13 |
| State | Published - May 5 1990 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
Cite this
Kinetic studies on the mechanism and regulation of rabbit liver fructose-1,6-bisphosphatase. / Liu, Feng; Fromm, Herbert J.
In: Journal of Biological Chemistry, Vol. 265, No. 13, 05.05.1990, p. 7401-7406.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Kinetic studies on the mechanism and regulation of rabbit liver fructose-1,6-bisphosphatase
AU - Liu, Feng
AU - Fromm, Herbert J.
PY - 1990/5/5
Y1 - 1990/5/5
N2 - The interaction of Mg2+, AMP, and fructose 2,6-bisphosphate with respect to rabbit liver fructose-1,6-bisphosphatase was investigated by studying initial-rate kinetics of the system at pH 9.5. A rapid-equilibrium Random Bi Bi mechanism is suggested for the rabbit liver enzyme from the kinetic data. Our kinetic findings indicate that Mg2+ and the inhibitor AMP are mutually exclusive in their binding to fructose-1,6-bisphosphatase. This probably is the mechanism for AMP regulation of fructose-1,6-bisphosphatase and thus, to some extent, gluconeogenesis. A kinetic model for the interaction of these ligands with respect to rabbit liver fructose-1,6-bisphosphatase is presented.
AB - The interaction of Mg2+, AMP, and fructose 2,6-bisphosphate with respect to rabbit liver fructose-1,6-bisphosphatase was investigated by studying initial-rate kinetics of the system at pH 9.5. A rapid-equilibrium Random Bi Bi mechanism is suggested for the rabbit liver enzyme from the kinetic data. Our kinetic findings indicate that Mg2+ and the inhibitor AMP are mutually exclusive in their binding to fructose-1,6-bisphosphatase. This probably is the mechanism for AMP regulation of fructose-1,6-bisphosphatase and thus, to some extent, gluconeogenesis. A kinetic model for the interaction of these ligands with respect to rabbit liver fructose-1,6-bisphosphatase is presented.
UR - http://www.scopus.com/inward/record.url?scp=0025275124&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025275124&partnerID=8YFLogxK
M3 - Article
VL - 265
SP - 7401
EP - 7406
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 13
ER -