Ontology highlight
ABSTRACT:
SUBMITTER: Pluta P
PROVIDER: S-EPMC6192514 | biostudies-literature | 2018 Sep
REPOSITORIES: biostudies-literature
Pluta Paula P Roversi Pietro P Bernardo-Seisdedos Ganeko G Rojas Adriana L AL Cooper Jonathan B JB Gu Shuang S Pickersgill Richard W RW Millet Oscar O
Biochimica et biophysica acta. General subjects 20180615 9
Human porphobilinogen deaminase (PBGD), the third enzyme in the heme pathway, catalyzes four times a single reaction to convert porphobilinogen into hydroxymethylbilane. Remarkably, PBGD employs a single active site during the process, with a distinct yet chemically equivalent bond formed each time. The four intermediate complexes of the enzyme have been biochemically validated and they can be isolated but they have never been structurally characterized other than the apo- and holo-enzyme bound ...[more]