ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Crystallization and preliminary X-ray analysis of L-azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed, 6 citations in OpenAlex.
- A highly conserved mechanism for the detoxification and assimilation of the toxic phytoproduct L-azetidine-2-carboxylic acid in Aspergillus nidulans.Scientific reports · 2021Article
- Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.Current opinion in structural biology · 2011Review
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6 authors at 3 institutions in 2 countries.
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Abstract
L-Azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C catalyzes a ring-opening reaction that detoxifies L-azetidine-2-carboxylate, an analogue of L-proline. Recombinant L-azetidine-2-carboxylate hydrolase was overexpressed, purified and crystallized using polyethylene glycol and magnesium acetate as precipitants. The needle-shaped crystal belonged to space group P2(1), with unit-cell parameters a = 35.6, b = 63.6, c = 54.7 A, beta = 105.5 degrees . The crystal diffracted to a resolution of 1.38 A. The calculated V(M) value was 2.2 A(3) Da(-1), suggesting that the crystal contains one enzyme subunit in the asymmetric unit.
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