p-TPH Anticuerpo(Ser 58): sc-135716

---

Phenylalanine hydroxylase (PAH), tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) comprise a small family of monooxygenases that use tetrahydropterine as a cofactor during the catabolism of aromatic L-amino acids (1,2). PAH, TH and TPH all contain catalytic domains with an amino-terminal regulatory domain and a short carboxy-terminal tetramerization domain (1). Each of these enzymes also contains a single ferrous iron atom, which is bound to two histidines and a glutamate and is likely to be involved in the formation of the hydroxylating intermediate (1). TPH is the first and rate-limiting step in the biosynthesis of serotonin in the central nervous system and melatonin in the pineal gland (1-5). Alteration of TPH function may be a key factor in the pathology of several neuropsychiatric disorders associated with serotonin, including depression, aggression, alcoholism and schizophrenia (3,4,6,7). For instance, L-DOPA, which is used as a common therapy for Parkinson’s disease (PD) patients, inhibits TPH function, which subsequently, is thought to contribute to the onset of depression in PD patients (3,4). Mouse, rat, human and rabbit TPH undergo PKA-mediated phosphorylation on Ser 58, a residue that is located in the N-terminal regulatory domain.