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Bacillus megaterium CYP102A1 oxidation of acyl homoserine lactones and acyl homoserines.
- Source :
-
Biochemistry [Biochemistry] 2007 Dec 18; Vol. 46 (50), pp. 14429-37. Date of Electronic Publication: 2007 Nov 20. - Publication Year :
- 2007
-
Abstract
- Quorum sensing, the ability of bacteria to sense their own population density through the synthesis and detection of small molecule signals, has received a great deal of attention in recent years. Acyl homoserine lactones (AHLs) are a major class of quorum sensing signaling molecules. In nature, some bacteria that do not synthesize AHLs themselves have developed the ability to degrade these compounds by cleaving the amide bond or the lactone ring. By inactivating this signal used by competing bacteria, the degrading microbe is believed to gain a competitive advantage. In this work we report that CYP102A1, a widely studied cytochrome P450 from Bacillus megaterium, is capable of very efficient oxidation of AHLs and their lactonolysis products acyl homoserines. The previously known substrates for this enzyme, fatty acids, can also be formed in nature by hydrolysis of the amide of AHLs, so CYP102A1 is capable of inactivating the active parent compound and the products of both known pathways for AHL inactivation observed in nature. AHL oxidation primarily takes place at the omega-1, omega-2, and omega-3 carbons of the acyl chain, similar to this enzyme's well-known activity on fatty acids. Acyl homoserines and their lactones are better substrates for CYP102A1 than fatty acids. Bioassay of the quorum sensing activity of oxidation products reveals that the subterminally hydroxylated AHLs exhibit quorum sensing activity, but are 18-fold less active than the parent compound. In vivo, B. megaterium inactivates AHLs by a CYP102A1 dependent mechanism that must involve additional components that further sequester or metabolize the products, eliminating their quorum sensing activity. Cytochrome P450 oxidation of AHLs represents an important new mechanism of quorum quenching.
- Subjects :
- Acyl-Butyrolactones chemistry
Bacillus megaterium enzymology
Gas Chromatography-Mass Spectrometry
Homoserine chemistry
Kinetics
Molecular Structure
NADPH-Ferrihemoprotein Reductase
Oxidation-Reduction
Protein Binding
Quorum Sensing
Acyl-Butyrolactones metabolism
Bacillus megaterium metabolism
Bacterial Proteins metabolism
Cytochrome P-450 Enzyme System metabolism
Homoserine metabolism
Mixed Function Oxygenases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-2960
- Volume :
- 46
- Issue :
- 50
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 18020460
- Full Text :
- https://doi.org/10.1021/bi701945j