Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.7.11.12 (
PKG
)
2,515
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Brain aromatic L-amino acid decarboxylase (AAAD) is subject to regulation, and phosphorylation might be involved in the short-term activation of the enzyme. Sites for serine/threonine phosphorylation are present in the deduced amino acid sequence of AAAD, and cAMP-dependent protein kinase phosphorylates and activates neuronal AAAD in vitro. We now report that
cGMP-dependent protein kinase
(
PKG
) is able to phosphorylate and activate neuronal AAAD. In an in vitro kinase assay, immunoprecipitated native and recombinant mouse brain AAAD was rapidly phosphorylated by exogenous PKGIalpha. When added to striatal homogenates, PKGIalpha increased AAAD activity in a temporal fashion similar to phosphorylation. Recombinant AAAD was also activated by the kinase demonstrating a direct effect. Native enzyme activation was moderate and characterized by increased V(max) and K(m) for
L-DOPA
. A
PKG
peptide inhibitor prevented AAAD phosphorylation and activation providing specificity, and causally linking the two events. Together, the findings provide evidence for PKGIalpha-dependent phosphorylation and activation of neuronal AAAD in vitro, and introduce AAAD as a putative PKGIalpha substrate. Neuronal AAAD is best known for its role in the biosynthesis of catecholamines, indoleamines and trace amines in the nervous system, and the biological importance of PKGIalpha phosphorylation in these processes remains to be determined.
...
PMID:Aromatic L-amino acid decarboxylase phosphorylation and activation by PKGIalpha in vitro. 2045 15
