Functional analysis of iodotyrosine deiodinase from drosophila melanogaster.

ABSTRACT: The flavoprotein iodotyrosine deiodinase (IYD) was first discovered in mammals through its ability to salvage iodide from mono- and diiodotyrosine, the by-products of thyroid hormone synthesis. Genomic information indicates that invertebrates contain homologous enzymes although their iodide requirements are unknown. The catalytic domain of IYD from Drosophila melanogaster has now been cloned, expressed and characterized to determine the scope of its potential catalytic function as a model for organisms that are not associated with thyroid hormone production. Little discrimination between iodo-, bromo-, and chlorotyrosine was detected. Their affinity for IYD ranges from 0.46 to 0.62 μM (K_d ) and their efficiency of dehalogenation ranges from 2.4 - 9 x 10³ M^-1

SUBMITTER: Phatarphekar A 

PROVIDER: S-EPMC5119571 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature