期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 66, 期 -, 页码 1045-1049出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S174430911002748X
关键词
bacterial monooxygenases; phenylacetic acid; coenzyme A; aerobic metabolism of aromatic compounds
资金
- Canadian Institutes of Health Research [GSP-48370]
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 similar to 2.0 A resolution. PaaAC represents the first crystallized BMM hydroxylase that utilizes a CoA-linked substrate.
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