5hft
From Proteopedia
Crystal structure of HpxW
Structural highlights
FunctionHPXW_KLEP7 Involved in the uric acid degradation pathway. Catalyzes the conversion of oxamate to oxalate.[1] Publication Abstract from PubMedHpxW 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. Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway.,Hicks KA, Ealick SE Acta Crystallogr D Struct Biol. 2016 Jun 1;72(Pt 6):808-16. doi:, 10.1107/S2059798316007099. Epub 2016 May 25. PMID:27303801[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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