Literature summary for 3.5.2.2 extracted from

Abendroth, J.; Niefind, K.; Schomburg, D.
X-ray structure of a dihydropyrimidinase from Thermus sp. at 1.3 A resolution (2002), J. Mol. Biol., 320, 143-156.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Thermus sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals are grown using the sitting-drop, vapour-diffusion method. C2221 crystals are grown with 1.65 M ammonium sulfate, 5% PEG 400, 100 mM HepesNaOH (pH 7.5). The crystal structure is solved by multiwavelength anomalous diffraction phasing. The structure is refined at 1.30 A resolution. The core of D-hydantoinase consists of a (alpha/beta)(8)-barrel, which is flanked by a beta-sheet domain and some additional helices. In the active site, a carboxylated lysine residue and the catalytically active hydroxide ion bridge a binuclear zinc centre	Thermus sp.

Crystallization (Comment)

Organism

crystals are grown using the sitting-drop, vapour-diffusion method. C2221 crystals are grown with 1.65 M ammonium sulfate, 5% PEG 400, 100 mM HepesNaOH (pH 7.5). The crystal structure is solved by multiwavelength anomalous diffraction phasing. The structure is refined at 1.30 A resolution. The core of D-hydantoinase consists of a (alpha/beta)(8)-barrel, which is flanked by a beta-sheet domain and some additional helices. In the active site, a carboxylated lysine residue and the catalytically active hydroxide ion bridge a binuclear zinc centre

Thermus sp.

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	in the active site, a carboxylated lysine residue and the catalytically active hydroxide ion bridge a binuclear zinc centre	Thermus sp.

Organism

Organism	UniProt	Comment	Textmining
Thermus sp.	Q7SIE9	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Thermus sp.

Synonyms

Synonyms	Comment	Organism
D-hydantoinase	-	Thermus sp.
hydantoinase	-	Thermus sp.

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Release 2023.1 (January 2023)