5NNB

Isatin hydrolase A (IHA) from Labrenzia aggregata with isatinate bound

5NNB の概要

• エントリーDOI: 10.2210/pdb5nnb/pdb
• 分子名称: isatin hydrolase A, MANGANESE (II) ION, Isatinic acid, ... (4 entities in total)
• 機能のキーワード: isatin, hydrolase, labrenzia aggregata, isatinate
• 由来する生物種: Labrenzia aggregata
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 112533.03

構造登録者

Sommer, T.,Bjerregaard-Andersen, K.,Morth, J.P. (登録日: 2017-04-08, 公開日: 2018-05-16, 最終更新日: 2024-01-17)

主引用文献

Sommer, T.,Bjerregaard-Andersen, K.,Uribe, L.,Etzerodt, M.,Diezemann, G.,Gauss, J.,Cascella, M.,Morth, J.P.
A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase.
Sci Rep, 8:13104-13104, 2018

PubMed Abstract: The catalytic mechanism of the cyclic amidohydrolase isatin hydrolase depends on a catalytically active manganese in the substrate-binding pocket. The Mn ion is bound by a motif also present in other metal dependent hydrolases like the bacterial kynurenine formamidase. The crystal structures of the isatin hydrolases from Labrenzia aggregata and Ralstonia solanacearum combined with activity assays allow for the identification of key determinants specific for the reaction mechanism. Active site residues central to the hydrolytic mechanism include a novel catalytic triad Asp-His-His supported by structural comparison and hybrid quantum mechanics/classical mechanics simulations. A hydrolytic mechanism for a Mn dependent amidohydrolases that disfavour Zn as the primary catalytically active site metal proposed here is supported by these likely cases of convergent evolution. The work illustrates a fundamental difference in the substrate-binding mode between Mn dependent isatin hydrolase like enzymes in comparison with the vast number of Zn dependent enzymes.

PubMed: 30166577
DOI: 10.1038/s41598-018-31259-y

実験手法

X-RAY DIFFRACTION (1.8 Å)