Stabilization of tryptophan hydroxylase 2 by l-phenylalanine-induced dimerization.

ABSTRACT: Tryptophan hydroxylase 2 (TPH2) catalyses the initial and rate-limiting step in the biosynthesis of serotonin, which is associated with a variety of disorders such as depression, obsessive compulsive disorder, and schizophrenia. Full-length TPH2 is poorly characterized due to low purification quantities caused by its inherent instability. Three truncated variants of human TPH2 (rch TPH2; regulatory and catalytic domain, NΔ47-rch TPH2; truncation of 47 residues in the N terminus of rch TPH2, and ch TPH2; catalytic domain) were expressed, purified, and examined for changes in transition temperature, inactivation rate, and oligomeric state. ch TPH2 displayed 14- and 11-fold higher half-lives compared to rch TPH2 and NΔ47-rch TPH2, respectively.

SUBMITTER: Tidemand KD 

PROVIDER: S-EPMC5055035 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature