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5hft
From Proteopedia
(Difference between revisions)
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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 == | ||
| - | 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 class="pdbe-citations 5hft" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of HpxW
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