Literature summary for 3.5.2.2 extracted from

Zhang, X.; Yuan, J.; Niu, L.; Liang, A.
Quantitative analysis and functional evaluation of zinc ion in the D-hydantoinase from Pseudomonas putida YZ-26 (2010), Biometals, 23, 71-81.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pseudomonas putida

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zinc	in vitro preparation of apo-HDT, i.e. metal-removed HDT, and Zn2+-HDT, i.e. Zn2+-added HDT. The Zn2+-HDT and re-HDT contain 2.17 and 0.95 mol Zn2+ per mol subunit, respectively, and have comparable enzymatic activities. In contrast, the apo-HDT only retains 0.04 mol Zn2+ per mol subunit with less than 10% activity, compared with the re-HDT. When the apo-HDT is reconstituted with ZnCl2, the enzymatic activity recovery is about 75%. Data suggest that the re-HDT may have two Zn2+-binding sites, one is an intrinsic or tight-binding site, zinc-alpha, essential for its activity and the other is a vacant or loose-binding site, zinc-beta, possibly non-essential for the activity	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	strain YZ-26	-

Renatured (Commentary)

Renatured (Comment)	Organism
when the apo-HDT depleted of zinc is reconstituted with ZnCl2, the enzymatic activity recovery is about 75%	Pseudomonas putida

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Release 2023.1 (January 2023)