FN Archimer Export Format
PT J
TI Proteomic investigation of enzymes involved in 2-ethylhexyl nitrate biodegradation in Mycobacterium austroafricanum IFP 2173
BT 
AF NICOLAU, Elodie
   KUHN, Lauriane
   MARCHAL, Remy
   JOUANNEAU, Yves
AS 1:1,3,4;2:2;3:4;4:1,3;
FF 1:;2:;3:;4:;
C1 Laboratoire de Chimie et Biologie des Métaux, CEA, iRTSV, 17, rue des Martyrs, 38054 Grenoble, France
   Laboratoire d'Etude de la Dynamique des Protéomes, CEA, iRTSV, 38054 Grenoble, France
   CNRS-UMR5249, 38054 Grenoble, France
   Département de Biotechnologie, Institut Français du Pétrole, 92852 Rueil-Malmaison Cedex, France
C2 CEA, FRANCE
   CEA, FRANCE
   CNRS, FRANCE
   IFP, FRANCE
IF 2.154
TC 9
UR https://archimer.ifremer.fr/doc/00815/92746/99295.pdf
LA English
DT Article
DE ;Alkane hydroxylase;Cytochrome P450;CYP153;2-Ethylhexyl nitrate;Mycobacterium austroafricanum;beta-oxidation
AB 2-Ethyhexyl nitrate (2-EHN) is a synthetic chemical used as a diesel fuel additive, which is recalcitrant to biodegradation. In this study, the enzymes involved in 2-EHN degradation were investigated in Mycobacterium austroafricanum IFP 2173. Using two-dimensional gel electrophoresis and a shotgun proteomic approach, a total of 398 proteins appeared to be more abundant in cells exposed to 2-EHN than in acetate-grown cells. This set of proteins includes multiple isoenzymes of the beta-oxidation pathway, two alcohol and one aldehyde dehydrogenase, as well as four cytochromes P450, including one CYP153 which functions as an alkane hydroxylase. Strain IFP 2173 was also found to contain two alkB-like genes encoding putative membrane-bound alkane hydroxylases. RT-PCR experiments showed that the gene encoding the CYP153 protein, as well as alkB genes, were expressed on 2-EHN. These findings are discussed in the light of a recently proposed 2-EHN degradation pathway involving an initial attack by an alkane hydroxylase and one turn of beta-oxidation, leading to the accumulation of a gamma-lactone as a deadend product. 
PY 2009
PD DEC
SO Research In Microbiology
SN 0923-2508
PU Elsevier Science Bv
VL 160
IS 10
UT 000273233200014
BP 838
EP 847
DI 10.1016/j.resmic.2009.09.017
ID 92746
ER

EF