Ontology highlight
ABSTRACT:
SUBMITTER: Hicks KA
PROVIDER: S-EPMC4908869 | biostudies-literature | 2016 Jun
REPOSITORIES: biostudies-literature

Hicks Katherine A KA Ealick Steven E SE
Acta crystallographica. Section D, Structural biology 20160525 Pt 6
HpxW from the ubiquitous pathogen Klebsiella pneumoniae is involved in a novel uric acid degradation pathway downstream from the formation of oxalurate. Specifically, HpxW is an oxamate amidohydrolase which catalyzes the conversion of oxamate to oxalate and is a member of the Ntn-hydrolase superfamily. HpxW is autoprocessed from an inactive precursor to form a heterodimer, resulting in a 35.5 kDa α subunit and a 20 kDa β subunit. Here, the structure of HpxW is presented and the substrate complex ...[more]