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Identification and characterization of 2-naphthoyl-coenzyme A reductase, the prototype of a novel class of dearomatizing reductases.
- Source :
-
Molecular microbiology [Mol Microbiol] 2013 Jun; Vol. 88 (5), pp. 1032-9. Date of Electronic Publication: 2013 May 07. - Publication Year :
- 2013
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Abstract
- The enzymatic dearomatization of aromatic ring systems by reduction represents a highly challenging redox reaction in biology and plays a key role in the degradation of aromatic compounds under anoxic conditions. In anaerobic bacteria, most monocyclic aromatic growth substrates are converted to benzoyl-coenzyme A (CoA), which is then dearomatized to a conjugated dienoyl-CoA by ATP-dependent or -independent benzoyl-CoA reductases. It was unresolved whether or not related enzymes are involved in the anaerobic degradation of environmentally relevant polycyclic aromatic hydrocarbons (PAHs). In this work, a previously unknown dearomatizing 2-naphthoyl-CoA reductase was purified from extracts of the naphthalene-degrading, sulphidogenic enrichment culture N47. The oxygen-tolerant enzyme dearomatized the non-activated ring of 2-naphthoyl-CoA by a four-electron reduction to 5,6,7,8-tetrahydro-2-naphthoyl-CoA. The dimeric 150 kDa enzyme complex was composed of a 72 kDa subunit showing sequence similarity to members of the flavin-containing 'old yellow enzyme' family. NCR contained FAD, FMN, and an iron-sulphur cluster as cofactors. Extracts of Escherichia coli expressing the encoding gene catalysed 2-naphthoyl-CoA reduction. The identified NCR is a prototypical enzyme of a previously unknown class of dearomatizing arylcarboxyl-CoA reductases that are involved in anaerobic PAH degradation; it fundamentally differs from known benzoyl-CoA reductases.<br /> (© 2013 John Wiley & Sons Ltd.)
- Subjects :
- Anaerobiosis
Biotransformation
Coenzymes metabolism
Environmental Microbiology
Escherichia coli genetics
Flavin Mononucleotide metabolism
Flavin-Adenine Dinucleotide metabolism
Iron-Sulfur Proteins
Molecular Weight
Oxidoreductases chemistry
Oxidoreductases isolation & purification
Protein Multimerization
Recombinant Proteins genetics
Recombinant Proteins metabolism
Carboxylic Acids metabolism
Coenzyme A metabolism
Naphthalenes metabolism
Oxidoreductases genetics
Oxidoreductases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1365-2958
- Volume :
- 88
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Molecular microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 23646996
- Full Text :
- https://doi.org/10.1111/mmi.12238