Abstract
The catalytic subunit of protein kinase A increases brain tryptophan hydroxylase activity. The activation is manifested as an increase in V(max) without alterations in the K(m) for either tetrahydrobiopterin or tryptophan. The activation of tryptophan hydroxylase by protein kinase A is dependent on ATP and an intact kinase and is inhibited specifically by protein kinase A inhibitors. Protein kinase A also catalyzes the phosphorylation of tryptophan hydroxylase. The extent to which tryptophan hydroxylase is phosphorylated by protein kinase A is dependent on the amount of kinase used and is closely related to the degree to which the hydroxylase is activated. These results suggest that a direct relationship exists between phosphorylation and activation of tryptophan hydroxylase by protein kinase A.
| Original language | English |
|---|---|
| Pages (from-to) | 817-823 |
| Number of pages | 7 |
| Journal | Journal of Neurochemistry |
| Volume | 66 |
| Issue number | 2 |
| Publication status | Published - 1 Feb 1996 |
| Externally published | Yes |
Keywords
- Activation
- Phosphorylation
- Protein kinase A
- Tryptophan hydroxylase
Cite this
}
Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A. / Johansen, Patricia A.; Jennings, Ian; Cotton, Richard G H; Kuhn, Donald M.
In: Journal of Neurochemistry, Vol. 66, No. 2, 01.02.1996, p. 817-823.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A
AU - Johansen, Patricia A.
AU - Jennings, Ian
AU - Cotton, Richard G H
AU - Kuhn, Donald M.
PY - 1996/2/1
Y1 - 1996/2/1
N2 - The catalytic subunit of protein kinase A increases brain tryptophan hydroxylase activity. The activation is manifested as an increase in V(max) without alterations in the K(m) for either tetrahydrobiopterin or tryptophan. The activation of tryptophan hydroxylase by protein kinase A is dependent on ATP and an intact kinase and is inhibited specifically by protein kinase A inhibitors. Protein kinase A also catalyzes the phosphorylation of tryptophan hydroxylase. The extent to which tryptophan hydroxylase is phosphorylated by protein kinase A is dependent on the amount of kinase used and is closely related to the degree to which the hydroxylase is activated. These results suggest that a direct relationship exists between phosphorylation and activation of tryptophan hydroxylase by protein kinase A.
AB - The catalytic subunit of protein kinase A increases brain tryptophan hydroxylase activity. The activation is manifested as an increase in V(max) without alterations in the K(m) for either tetrahydrobiopterin or tryptophan. The activation of tryptophan hydroxylase by protein kinase A is dependent on ATP and an intact kinase and is inhibited specifically by protein kinase A inhibitors. Protein kinase A also catalyzes the phosphorylation of tryptophan hydroxylase. The extent to which tryptophan hydroxylase is phosphorylated by protein kinase A is dependent on the amount of kinase used and is closely related to the degree to which the hydroxylase is activated. These results suggest that a direct relationship exists between phosphorylation and activation of tryptophan hydroxylase by protein kinase A.
KW - Activation
KW - Phosphorylation
KW - Protein kinase A
KW - Tryptophan hydroxylase
UR - http://www.scopus.com/inward/record.url?scp=0030050954&partnerID=8YFLogxK
M3 - Article
C2 - 8592157
AN - SCOPUS:0030050954
VL - 66
SP - 817
EP - 823
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
SN - 0022-3042
IS - 2
ER -