Abstract
In Pseudomonas putida U, the degradation of n-alkanoic and n-phenylalkanoic acids is carried out by two sets of β-oxidation enzymes (βI and βII). Whereas the first one (called βI) is constitutive and catalyses the degradation of n-alkanoic and n-phenylalkanoic acids very efficiently, the other one (βII), which is only expressed when some of the genes encoding βI enzymes are mutated, catabolizes n-phenylalkanoates (n > 4) much more slowly. Genetic studies revealed that disruption or deletion of some of the βI genes handicaps the growth of P. putida U in media containing n-alkanoic or n-phenylalkanoic acids with an acyl moiety longer than C4. However, all these mutants regained their ability to grow in media containing n-alkanoates as a result of the induction of βII, but they were still unable to catabolize n-phenylalkanoates completely, as the βI-FadBA enzymes are essential for the β-oxidation of certain n-phenylalkanoyl-CoA derivatives when they reach a critical size. Owing to the existence of the βII system, mutants lacking βI-fadB/A are able to synthesize new poly 3-OH-n-alkanoates (PHAs) and poly 3-OH-n-phenylalkanoates (PHPhAs) efficiently. However, they are unable to degrade these polymers, becoming bioplastic overproducer mutants. The genetic and biochemical importance of these results is reported and discussed.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 863-874 |
| Number of pages | 12 |
| Journal | Molecular Microbiology |
| Volume | 39 |
| Issue number | 4 |
| DOIs | |
| State | Published - Mar 8 2001 |
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ASJC Scopus subject areas
- Microbiology
- Molecular Biology
Cite this
Two different pathways are involved in the β-oxidation of n-alkanoic and n-phenylalkanoic acids in Pseudomonas putida U : Genetic studies and biotechnological applications. / Olivera, Elías R.; Carnicero, David; García, Belén; Miñambres, Baltasar; Moreno, Miguel A.; Cañedo, Librada; DiRusso, Concetta C.; Naharro, Germán; Luengo, José M.
In: Molecular Microbiology, Vol. 39, No. 4, 08.03.2001, p. 863-874.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Two different pathways are involved in the β-oxidation of n-alkanoic and n-phenylalkanoic acids in Pseudomonas putida U
T2 - Genetic studies and biotechnological applications
AU - Olivera, Elías R.
AU - Carnicero, David
AU - García, Belén
AU - Miñambres, Baltasar
AU - Moreno, Miguel A.
AU - Cañedo, Librada
AU - DiRusso, Concetta C.
AU - Naharro, Germán
AU - Luengo, José M.
PY - 2001/3/8
Y1 - 2001/3/8
N2 - In Pseudomonas putida U, the degradation of n-alkanoic and n-phenylalkanoic acids is carried out by two sets of β-oxidation enzymes (βI and βII). Whereas the first one (called βI) is constitutive and catalyses the degradation of n-alkanoic and n-phenylalkanoic acids very efficiently, the other one (βII), which is only expressed when some of the genes encoding βI enzymes are mutated, catabolizes n-phenylalkanoates (n > 4) much more slowly. Genetic studies revealed that disruption or deletion of some of the βI genes handicaps the growth of P. putida U in media containing n-alkanoic or n-phenylalkanoic acids with an acyl moiety longer than C4. However, all these mutants regained their ability to grow in media containing n-alkanoates as a result of the induction of βII, but they were still unable to catabolize n-phenylalkanoates completely, as the βI-FadBA enzymes are essential for the β-oxidation of certain n-phenylalkanoyl-CoA derivatives when they reach a critical size. Owing to the existence of the βII system, mutants lacking βI-fadB/A are able to synthesize new poly 3-OH-n-alkanoates (PHAs) and poly 3-OH-n-phenylalkanoates (PHPhAs) efficiently. However, they are unable to degrade these polymers, becoming bioplastic overproducer mutants. The genetic and biochemical importance of these results is reported and discussed.
AB - In Pseudomonas putida U, the degradation of n-alkanoic and n-phenylalkanoic acids is carried out by two sets of β-oxidation enzymes (βI and βII). Whereas the first one (called βI) is constitutive and catalyses the degradation of n-alkanoic and n-phenylalkanoic acids very efficiently, the other one (βII), which is only expressed when some of the genes encoding βI enzymes are mutated, catabolizes n-phenylalkanoates (n > 4) much more slowly. Genetic studies revealed that disruption or deletion of some of the βI genes handicaps the growth of P. putida U in media containing n-alkanoic or n-phenylalkanoic acids with an acyl moiety longer than C4. However, all these mutants regained their ability to grow in media containing n-alkanoates as a result of the induction of βII, but they were still unable to catabolize n-phenylalkanoates completely, as the βI-FadBA enzymes are essential for the β-oxidation of certain n-phenylalkanoyl-CoA derivatives when they reach a critical size. Owing to the existence of the βII system, mutants lacking βI-fadB/A are able to synthesize new poly 3-OH-n-alkanoates (PHAs) and poly 3-OH-n-phenylalkanoates (PHPhAs) efficiently. However, they are unable to degrade these polymers, becoming bioplastic overproducer mutants. The genetic and biochemical importance of these results is reported and discussed.
UR - http://www.scopus.com/inward/record.url?scp=0035117157&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035117157&partnerID=8YFLogxK
U2 - 10.1046/j.1365-2958.2001.02296.x
DO - 10.1046/j.1365-2958.2001.02296.x
M3 - Article
C2 - 11251808
AN - SCOPUS:0035117157
VL - 39
SP - 863
EP - 874
JO - Molecular Microbiology
JF - Molecular Microbiology
SN - 0950-382X
IS - 4
ER -