Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase.

ABSTRACT:

Background

3,4-Dihydroxyphenylalanine decarboxylase (DDC), also known as aromatic L-amino acid decarboxylase, catalyzes the decarboxylation of a number of aromatic L-amino acids. Physiologically, DDC is responsible for the production of dopamine and serotonin through the decarboxylation of 3,4-dihydroxyphenylalanine and 5-hydroxytryptophan, respectively. In insects, both dopamine and serotonin serve as classical neurotransmitters, neuromodulators, or neurohormones, and dopamine is also involved in insect cuticle formation, eggshell hardening, and immune responses.

Principal findings

In this study, we expressed a typical DDC enzyme from Drosophila melanogaster, critically analyzed its substrate specificity and biochemical properties, determined its crystal structure at 1.75 A

SUBMITTER: Han Q 

PROVIDER: S-EPMC2809104 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature