FadD from Pseudomonas putida CA-3 Is a True Long-Chain Fatty Acyl Coenzyme A Synthetase That Activates Phenylalkanoic and Alkanoic Acids
Апстракт
A fatty acyl coenzyme A synthetase (FadD) from Pseudomonas putida CA-3 is capable of activating a wide range of phenylalkanoic and alkanoic acids. It exhibits the highest rates of reaction and catalytic efficiency with long-chain aromatic and aliphatic substrates. FadD exhibits higher k(cat) and Km values for aromatic substrates than for the aliphatic equivalents (e. g., 15-phenylpentadecanoic acid versus pentadecanoic acid). FadD is inhibited noncompetitively by both acrylic acid and 2-bromooctanoic acid. The deletion of the fadD gene from P. putida CA-3 resulted in no detectable growth or polyhydroxyalkanoate (PHA) accumulation with 10-phenyldecanoic acid, decanoic acid, and longer-chain substrates. The results suggest that FadD is solely responsible for the activation of long-chain phenylalkanoic and alkanoic acids. While the CA-3 Delta fadD mutant could grow on medium-chain substrates, a decrease in growth yield and PHA accumulation was observed. The PHA accumulated by CA-3 Delta f...adD contained a greater proportion of short-chain monomers than did wild-type PHA. Growth of CA-3 Delta fadD was unaffected, but PHA accumulation decreased modestly with shorter-chain substrates. The complemented mutant regained 70% to 90% of the growth and PHA-accumulating ability of the wild-type strain depending on the substrate. The expression of an extra copy of fadD in P. putida CA-3 resulted in increased levels of PHA accumulation (up to 1.6-fold) and an increase in the incorporation of longer-monomer units into the PHA polymer.
Извор:
Journal of Bacteriology, 2009, 191, 24, 7554-7565Издавач:
- Amer Soc Microbiology, Washington
Финансирање / пројекти:
- University College Dublin
- Environmental Protection Agency Ireland [ERTDI 2005-ET-LS-9-M3]
DOI: 10.1128/JB.01016-09
ISSN: 0021-9193
PubMed: 19820085
WoS: 000272030400019
Scopus: 2-s2.0-72449189757
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Hume, Aisling R. AU - Nikodinović-Runić, Jasmina AU - O'Connor, Kevin PY - 2009 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/377 AB - A fatty acyl coenzyme A synthetase (FadD) from Pseudomonas putida CA-3 is capable of activating a wide range of phenylalkanoic and alkanoic acids. It exhibits the highest rates of reaction and catalytic efficiency with long-chain aromatic and aliphatic substrates. FadD exhibits higher k(cat) and Km values for aromatic substrates than for the aliphatic equivalents (e. g., 15-phenylpentadecanoic acid versus pentadecanoic acid). FadD is inhibited noncompetitively by both acrylic acid and 2-bromooctanoic acid. The deletion of the fadD gene from P. putida CA-3 resulted in no detectable growth or polyhydroxyalkanoate (PHA) accumulation with 10-phenyldecanoic acid, decanoic acid, and longer-chain substrates. The results suggest that FadD is solely responsible for the activation of long-chain phenylalkanoic and alkanoic acids. While the CA-3 Delta fadD mutant could grow on medium-chain substrates, a decrease in growth yield and PHA accumulation was observed. The PHA accumulated by CA-3 Delta fadD contained a greater proportion of short-chain monomers than did wild-type PHA. Growth of CA-3 Delta fadD was unaffected, but PHA accumulation decreased modestly with shorter-chain substrates. The complemented mutant regained 70% to 90% of the growth and PHA-accumulating ability of the wild-type strain depending on the substrate. The expression of an extra copy of fadD in P. putida CA-3 resulted in increased levels of PHA accumulation (up to 1.6-fold) and an increase in the incorporation of longer-monomer units into the PHA polymer. PB - Amer Soc Microbiology, Washington T2 - Journal of Bacteriology T1 - FadD from Pseudomonas putida CA-3 Is a True Long-Chain Fatty Acyl Coenzyme A Synthetase That Activates Phenylalkanoic and Alkanoic Acids EP - 7565 IS - 24 SP - 7554 VL - 191 DO - 10.1128/JB.01016-09 ER -
@article{ author = "Hume, Aisling R. and Nikodinović-Runić, Jasmina and O'Connor, Kevin ", year = "2009", abstract = "A fatty acyl coenzyme A synthetase (FadD) from Pseudomonas putida CA-3 is capable of activating a wide range of phenylalkanoic and alkanoic acids. It exhibits the highest rates of reaction and catalytic efficiency with long-chain aromatic and aliphatic substrates. FadD exhibits higher k(cat) and Km values for aromatic substrates than for the aliphatic equivalents (e. g., 15-phenylpentadecanoic acid versus pentadecanoic acid). FadD is inhibited noncompetitively by both acrylic acid and 2-bromooctanoic acid. The deletion of the fadD gene from P. putida CA-3 resulted in no detectable growth or polyhydroxyalkanoate (PHA) accumulation with 10-phenyldecanoic acid, decanoic acid, and longer-chain substrates. The results suggest that FadD is solely responsible for the activation of long-chain phenylalkanoic and alkanoic acids. While the CA-3 Delta fadD mutant could grow on medium-chain substrates, a decrease in growth yield and PHA accumulation was observed. The PHA accumulated by CA-3 Delta fadD contained a greater proportion of short-chain monomers than did wild-type PHA. Growth of CA-3 Delta fadD was unaffected, but PHA accumulation decreased modestly with shorter-chain substrates. The complemented mutant regained 70% to 90% of the growth and PHA-accumulating ability of the wild-type strain depending on the substrate. The expression of an extra copy of fadD in P. putida CA-3 resulted in increased levels of PHA accumulation (up to 1.6-fold) and an increase in the incorporation of longer-monomer units into the PHA polymer.", publisher = "Amer Soc Microbiology, Washington", journal = "Journal of Bacteriology", title = "FadD from Pseudomonas putida CA-3 Is a True Long-Chain Fatty Acyl Coenzyme A Synthetase That Activates Phenylalkanoic and Alkanoic Acids", pages = "7565-7554", number = "24", volume = "191", doi = "10.1128/JB.01016-09" }
Hume, A. R., Nikodinović-Runić, J.,& O'Connor, K.. (2009). FadD from Pseudomonas putida CA-3 Is a True Long-Chain Fatty Acyl Coenzyme A Synthetase That Activates Phenylalkanoic and Alkanoic Acids. in Journal of Bacteriology Amer Soc Microbiology, Washington., 191(24), 7554-7565. https://doi.org/10.1128/JB.01016-09
Hume AR, Nikodinović-Runić J, O'Connor K. FadD from Pseudomonas putida CA-3 Is a True Long-Chain Fatty Acyl Coenzyme A Synthetase That Activates Phenylalkanoic and Alkanoic Acids. in Journal of Bacteriology. 2009;191(24):7554-7565. doi:10.1128/JB.01016-09 .
Hume, Aisling R., Nikodinović-Runić, Jasmina, O'Connor, Kevin , "FadD from Pseudomonas putida CA-3 Is a True Long-Chain Fatty Acyl Coenzyme A Synthetase That Activates Phenylalkanoic and Alkanoic Acids" in Journal of Bacteriology, 191, no. 24 (2009):7554-7565, https://doi.org/10.1128/JB.01016-09 . .