5HFT

Crystal structure of HpxW

5HFT の概要

• エントリーDOI: 10.2210/pdb5hft/pdb
• 分子名称: Gamma-glutamyltranspeptidase (2 entities in total)
• 機能のキーワード: amidohydrolase, transferase
• 由来する生物種: Klebsiella pneumoniae subsp. pneumoniae; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 116603.31

構造登録者

Ealick, S.E.,Hicks, K.A. (登録日: 2016-01-07, 公開日: 2016-06-29, 最終更新日: 2024-03-06)

主引用文献

Hicks, K.A.,Ealick, S.E.
Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway.
Acta Crystallogr D Struct Biol, 72:808-816, 2016

PubMed Abstract: 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.

PubMed: 27303801
DOI: 10.1107/S2059798316007099

実験手法

X-RAY DIFFRACTION (2.646 Å)