Ontology highlight
ABSTRACT:
SUBMITTER: Phillips JD
PROVIDER: S-EPMC291847 | biostudies-literature | 2003 Dec
REPOSITORIES: biostudies-literature
Phillips John D JD Whitby Frank G FG Kushner James P JP Hill Christopher P CP
The EMBO journal 20031201 23
Uroporphyrinogen decarboxylase (URO-D), an essential enzyme that functions in the heme biosynthetic pathway, catalyzes decarboxylation of all four acetate groups of uroporphyrinogen to form coproporphyrinogen. Here we report crystal structures of URO-D in complex with the I and III isomer coproporphyrinogen products. Crystallization required use of a novel enzymatic approach to generate the highly oxygen-sensitive porphyrinogen substrate in situ. The tetrapyrrole product adopts a domed conformat ...[more]