Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway.

Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway.
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尿酸降解途径中肺炎克雷伯菌草酸酰胺水解酶的生化和结构特征。

DOI:
10.1107/s2059798316007099
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发表时间:
2016
期刊:
Acta crystallographica. Section D, Structural biology
影响因子:
--
通讯作者:
Ealick,StevenE
Ealick,StevenE
中科院分区:
--
文献类型:
--
作者:
Hicks,KatherineA;Ealick,StevenE

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来自普遍存在的肺炎克雷伯菌的HpxW参与了草酸形成下游的一种新的尿酸降解途径。具体地说,HpxW是一种草酸氨基水解酶,催化草酸转化为草酸,是NTN-水解酶超家族的成员。HpxW是由不活跃的前体自动加工而成的杂二聚体,产生35.5kDa的 α亚基和20kDa的 β亚基。在这里,给出了HpxW的结构,并对衬底复合体进行了建模。此外,还对该酶和两个活性中心变异体的稳态动力学进行了表征。这些结构和生化研究提供了对这类酶的进一步了解,并允许提出一种与NTN-水解酶超家族其他成员一致的催化机制。
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 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.
幽门螺杆菌γ-谷氨酰转肽酶的自动加工导致苏氨酸-苏氨酸催化二元体的形成。
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影响因子: --
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