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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/HPXW_KLEP7 HPXW_KLEP7] Involved in the uric acid degradation pathway. Catalyzes the conversion of oxamate to oxalate.<ref>PMID:27303801</ref> | | [https://www.uniprot.org/uniprot/HPXW_KLEP7 HPXW_KLEP7] Involved in the uric acid degradation pathway. Catalyzes the conversion of oxamate to oxalate.<ref>PMID:27303801</ref> |
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| == Publication Abstract from PubMed ==
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| 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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| 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<ref>PMID:27303801</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5hft" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
