Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids
2014
Authors
Guzik, Maciej W.Narancić, Tanja
Ilić-Tomić, Tatjana
Vojnović, Sandra
Kenny, Shane T.
Casey, William T.
Duane, Gearoid F.
Casey, Eoin
Woods, Trevor
Babu, Ramesh
Nikodinović-Runić, Jasmina
O'Connor, Kevin
Article (Published version)
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Diverse and elaborate pathways for nutrient utilization, as well as mechanisms to combat unfavourable nutrient conditions make Pseudomonas putida KT2440 a versatile micro-organism able to occupy a range of ecological niches. The fatty acid degradation pathway of P. putida is complex and correlated with biopolymer medium chain length polyhydroxyalkanoate (mcl-PHA) biosynthesis. Little is known about the second step of fatty acid degradation (beta-oxidation) in this strain. In silico analysis of its genome sequence revealed 21 putative acyl-CoA dehydrogenases (ACADs), four of which were functionally characterized through mutagenesis studies. Four mutants with insertionally inactivated ACADs (PP_1893, PP_2039, PP_2048 and PP_2437) grew and accumulated mcl-PHA on a range of fatty acids as the sole source of carbon and energy. Their ability to grow and accumulate biopolymer was differentially negatively affected on various fatty acids, in comparison to the wild-type strain. Inactive PP_2437... exhibited a pattern of reduced growth and PHA accumulation when fatty acids with lengths of 10 to 14 carbon chains were used as substrates. Recombinant expression and biochemical characterization of the purified protein allowed functional annotation in P. putida KT2440 as an ACAD showing clear preference for dodecanoyl-CoA ester as a substrate and optimum activity at 30 degrees C and pH 6.5-7.
Source:
Microbiology-Sgm, 2014, 160, 1760-1771Publisher:
- Microbiology Soc, London
Funding / projects:
- Environmental Protection Agency of Ireland [2008-ET-LS1]
- Microbial diversity study and characterization of beneficial environmental microorganisms (RS-MESTD-Basic Research (BR or ON)-173048)
DOI: 10.1099/mic.0.078758-0
ISSN: 1350-0872
PubMed: 24794972
WoS: 000341678900019
Scopus: 2-s2.0-84905270409
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Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Guzik, Maciej W. AU - Narancić, Tanja AU - Ilić-Tomić, Tatjana AU - Vojnović, Sandra AU - Kenny, Shane T. AU - Casey, William T. AU - Duane, Gearoid F. AU - Casey, Eoin AU - Woods, Trevor AU - Babu, Ramesh AU - Nikodinović-Runić, Jasmina AU - O'Connor, Kevin PY - 2014 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/749 AB - Diverse and elaborate pathways for nutrient utilization, as well as mechanisms to combat unfavourable nutrient conditions make Pseudomonas putida KT2440 a versatile micro-organism able to occupy a range of ecological niches. The fatty acid degradation pathway of P. putida is complex and correlated with biopolymer medium chain length polyhydroxyalkanoate (mcl-PHA) biosynthesis. Little is known about the second step of fatty acid degradation (beta-oxidation) in this strain. In silico analysis of its genome sequence revealed 21 putative acyl-CoA dehydrogenases (ACADs), four of which were functionally characterized through mutagenesis studies. Four mutants with insertionally inactivated ACADs (PP_1893, PP_2039, PP_2048 and PP_2437) grew and accumulated mcl-PHA on a range of fatty acids as the sole source of carbon and energy. Their ability to grow and accumulate biopolymer was differentially negatively affected on various fatty acids, in comparison to the wild-type strain. Inactive PP_2437 exhibited a pattern of reduced growth and PHA accumulation when fatty acids with lengths of 10 to 14 carbon chains were used as substrates. Recombinant expression and biochemical characterization of the purified protein allowed functional annotation in P. putida KT2440 as an ACAD showing clear preference for dodecanoyl-CoA ester as a substrate and optimum activity at 30 degrees C and pH 6.5-7. PB - Microbiology Soc, London T2 - Microbiology-Sgm T1 - Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids EP - 1771 SP - 1760 VL - 160 DO - 10.1099/mic.0.078758-0 ER -
@article{ author = "Guzik, Maciej W. and Narancić, Tanja and Ilić-Tomić, Tatjana and Vojnović, Sandra and Kenny, Shane T. and Casey, William T. and Duane, Gearoid F. and Casey, Eoin and Woods, Trevor and Babu, Ramesh and Nikodinović-Runić, Jasmina and O'Connor, Kevin ", year = "2014", abstract = "Diverse and elaborate pathways for nutrient utilization, as well as mechanisms to combat unfavourable nutrient conditions make Pseudomonas putida KT2440 a versatile micro-organism able to occupy a range of ecological niches. The fatty acid degradation pathway of P. putida is complex and correlated with biopolymer medium chain length polyhydroxyalkanoate (mcl-PHA) biosynthesis. Little is known about the second step of fatty acid degradation (beta-oxidation) in this strain. In silico analysis of its genome sequence revealed 21 putative acyl-CoA dehydrogenases (ACADs), four of which were functionally characterized through mutagenesis studies. Four mutants with insertionally inactivated ACADs (PP_1893, PP_2039, PP_2048 and PP_2437) grew and accumulated mcl-PHA on a range of fatty acids as the sole source of carbon and energy. Their ability to grow and accumulate biopolymer was differentially negatively affected on various fatty acids, in comparison to the wild-type strain. Inactive PP_2437 exhibited a pattern of reduced growth and PHA accumulation when fatty acids with lengths of 10 to 14 carbon chains were used as substrates. Recombinant expression and biochemical characterization of the purified protein allowed functional annotation in P. putida KT2440 as an ACAD showing clear preference for dodecanoyl-CoA ester as a substrate and optimum activity at 30 degrees C and pH 6.5-7.", publisher = "Microbiology Soc, London", journal = "Microbiology-Sgm", title = "Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids", pages = "1771-1760", volume = "160", doi = "10.1099/mic.0.078758-0" }
Guzik, M. W., Narancić, T., Ilić-Tomić, T., Vojnović, S., Kenny, S. T., Casey, W. T., Duane, G. F., Casey, E., Woods, T., Babu, R., Nikodinović-Runić, J.,& O'Connor, K.. (2014). Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids. in Microbiology-Sgm Microbiology Soc, London., 160, 1760-1771. https://doi.org/10.1099/mic.0.078758-0
Guzik MW, Narancić T, Ilić-Tomić T, Vojnović S, Kenny ST, Casey WT, Duane GF, Casey E, Woods T, Babu R, Nikodinović-Runić J, O'Connor K. Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids. in Microbiology-Sgm. 2014;160:1760-1771. doi:10.1099/mic.0.078758-0 .
Guzik, Maciej W., Narancić, Tanja, Ilić-Tomić, Tatjana, Vojnović, Sandra, Kenny, Shane T., Casey, William T., Duane, Gearoid F., Casey, Eoin, Woods, Trevor, Babu, Ramesh, Nikodinović-Runić, Jasmina, O'Connor, Kevin , "Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids" in Microbiology-Sgm, 160 (2014):1760-1771, https://doi.org/10.1099/mic.0.078758-0 . .