期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 72, 期 -, 页码 808-816出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798316007099
关键词
Ntn-hydrolase superfamily; uric acid degradation; glutamyltranspeptidase; selenium SAD phasing
资金
- NIH [GM073220, GM103403]
- US Department of Energy, Office of Basic Energy Sciences [DE-AC02-06CH11357]
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 alpha subunit and a 20 kDa beta subunit. Here, the structure of HpxW is presented and the substrate complex is modeled. In addition, the steady-state kinetics of this enzyme and two active-site variants were characterized. These structural and biochemical studies provide further insight into this class of enzymes and allow a mechanism for catalysis consistent with other members of the Ntn-hydrolase superfamily to be proposed.
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