Open Accessα-synuclein enfolds tyrosine hydroxylase and dopamine ß-hydroxylase, potentially reducing dopamine and norepinephrine synthesis
Author(s) -
Steven Lehrer,
Peter H. Rheinstein
Publication year - 2022
Publication title -
journal of proteins and proteomics
Language(s) - English
Resource type - Journals
eISSN - 2524-4663
pISSN - 0975-8151
DOI - 10.1007/s42485-022-00088-z
Subject(s) - tyrosine hydroxylase , dopamine , aromatic l amino acid decarboxylase , protein data bank (rcsb pdb) , chemistry , tyrosine , norepinephrine , tyrosine 3 monooxygenase , biochemistry , biology , endocrinology
Parkinson's disease (PD) results from degeneration of dopamine and norepinephrine neurons due to α-synuclein aggregates that likely have their origin in the gut. Tyrosine hydroxylase (TH) catalyses the formation of L-DOPA, the rate-limiting step in the biosynthesis of dopamine. A second enzyme, DOPA decarboxylase (DDC), catalyzes the conversion of L-DOPA to dopamine. A third enzyme, dopamine ß-hydroxylase (DBH), catalyzes the conversion of dopamine to norepinephrine. To analyze possible interactions of α-synuclein with TH, DDC and DBH, we performed in silico protein-protein docking.