ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex.
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 3 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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3 citing papers in PubMed, 6 citations in OpenAlex.
- Review
- Epoxy Coenzyme A Thioester pathways for degradation of aromatic compounds.Applied and environmental microbiology · 2012Review
- Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex.The Journal of biological chemistry · 2011Article
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4 authors at 2 institutions in 1 country.
Funding
Abstract
The Escherichia coli paa operon encodes enzymes of the phenylacetic acid-utilization pathway that metabolizes phenylacetate in the form of a coenzyme A (CoA) derivative. The phenylacetyl-coenzyme A oxygenase complex, which has been postulated to contain five components designated PaaABCDE, catalyzes ring hydroxylation of phenylacetyl-CoA. The PaaAC subcomplex shows low sequence similarity to other bacterial multicomponent monooxygenases (BMMs) and forms a separate branch on the phylogenetic tree. PaaAC, which catalyzes the hydroxylation reaction, was purified and crystallized in the absence of a bound ligand as well as in complexes with CoA, 3-hydroxybutyryl-CoA, benzoyl-CoA and the true substrate phenylacetyl-CoA. Crystals of the ligand-free enzyme belonged to space group P2(1)2(1)2(1) and diffracted to 2.65 A resolution, whereas complexes with CoA and its derivatives crystallized in space group P4(1)2(1)2 and diffracted to approximately 2.0 A resolution. PaaAC represents the first crystallized BMM hydroxylase that utilizes a CoA-linked substrate.
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