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Literature summary extracted from

  • Guzik, M.W.; Narancic, T.; Ilic-Tomic, T.; Vojnovic, S.; Kenny, S.T.; Casey, W.T.; Duane, G.F.; Casey, E.; Woods, T.; Babu, R.P.; Nikodinovic-Runic, J.; OConnor, K.E.
    Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids (2014), Microbiology, 160, 1760-1771 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.8.7 expression in Escherichia coli Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.7 Pseudomonas putida Q88K54
-
-
1.3.8.7 Pseudomonas putida Q88L87
-
-
1.3.8.7 Pseudomonas putida Q88L96
-
-
1.3.8.7 Pseudomonas putida Q88LN6
-
-
1.3.8.7 Pseudomonas putida KT 2240 Q88K54
-
-
1.3.8.7 Pseudomonas putida KT 2240 Q88L87
-
-
1.3.8.7 Pseudomonas putida KT 2240 Q88L96
-
-
1.3.8.7 Pseudomonas putida KT 2240 Q88LN6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.7 decanoyl-CoA + electron transfer flavoprotein
-
 Pseudomonas putida decenoyl-CoA + reduced electron transfer flavoprotein
-
 ?
1.3.8.7 decanoyl-CoA + electron transfer flavoprotein
-
 Pseudomonas putida KT 2240 decenoyl-CoA + reduced electron transfer flavoprotein
-
 ?
1.3.8.7 dodecanoyl-CoA + electron transfer flavoprotein preferred substrate Pseudomonas putida dodecenoyl-CoA + reduced electron transfer flavoprotein
-
 ?
1.3.8.7 dodecanoyl-CoA + electron transfer flavoprotein preferred substrate Pseudomonas putida KT 2240 dodecenoyl-CoA + reduced electron transfer flavoprotein
-
 ?
1.3.8.7 additional information enzyme shows a preference towards esters of even chain length and very low activity with C3–C9 acyl-CoA esters as substrates Pseudomonas putida ?
-
 ?
1.3.8.7 additional information enzyme shows a preference towards esters of even chain length and very low activity with C3–C9 acyl-CoA esters as substrates Pseudomonas putida KT 2240 ?
-
 ?
1.3.8.7 tetradecanoyl-CoA + electron transfer flavoprotein
-
 Pseudomonas putida tetradecenoyl-CoA + reduced electron transfer flavoprotein
-
 ?
1.3.8.7 tetradecanoyl-CoA + electron transfer flavoprotein
-
 Pseudomonas putida KT 2240 tetradecenoyl-CoA + reduced electron transfer flavoprotein
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.8.7 ? x * 46000, SDS-PAGE Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
1.3.8.7 FadE
-
 Pseudomonas putida
1.3.8.7 PP_1893
-
 Pseudomonas putida
1.3.8.7 PP_2039
-
 Pseudomonas putida
1.3.8.7 PP_2048
-
 Pseudomonas putida
1.3.8.7 PP_2437
-
 Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.8.7 30
-
-
 Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.8.7 6.5 7
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.8.7 FAD
-
 Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.3.8.7 physiological function genome sequence reveals 21 putative acyl-CoA dehydrogenases. A mutant with insertionally inactivated isoform PP_1893 grows and accumulates medium chain length polyhydroxyalkanoate on a range of fatty acids as the sole source of carbon and energy Pseudomonas putida
1.3.8.7 physiological function genome sequence reveals 21 putative acyl-CoA dehydrogenases. A mutant with insertionally inactivated isoform PP_2039 grows and accumulates medium chain length polyhydroxyalkanoate on a range of fatty acids as the sole source of carbon and energy Pseudomonas putida
1.3.8.7 physiological function genome sequence reveals 21 putative acyl-CoA dehydrogenases. A mutant with insertionally inactivated isoform PP_2048 grows and accumulates medium chain length polyhydroxyalkanoate on a range of fatty acids as the sole source of carbon and energy Pseudomonas putida