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Literature summary for 1.3.8.7 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)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas putida

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
decanoyl-CoA + electron transfer flavoprotein
-
Pseudomonas putida decenoyl-CoA + reduced electron transfer flavoprotein
-
?
decanoyl-CoA + electron transfer flavoprotein
-
Pseudomonas putida KT 2240 decenoyl-CoA + reduced electron transfer flavoprotein
-
?
dodecanoyl-CoA + electron transfer flavoprotein preferred substrate Pseudomonas putida dodecenoyl-CoA + reduced electron transfer flavoprotein
-
?
dodecanoyl-CoA + electron transfer flavoprotein preferred substrate Pseudomonas putida KT 2240 dodecenoyl-CoA + reduced electron transfer flavoprotein
-
?
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 ?
-
?
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 ?
-
?
tetradecanoyl-CoA + electron transfer flavoprotein
-
Pseudomonas putida tetradecenoyl-CoA + reduced electron transfer flavoprotein
-
?
tetradecanoyl-CoA + electron transfer flavoprotein
-
Pseudomonas putida KT 2240 tetradecenoyl-CoA + reduced electron transfer flavoprotein
-
?

Subunits

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

Synonyms

Synonyms Comment Organism
FadE
-
Pseudomonas putida
PP_1893
-
Pseudomonas putida
PP_2039
-
Pseudomonas putida
PP_2048
-
Pseudomonas putida
PP_2437
-
Pseudomonas putida

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7
-
Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
FAD
-
Pseudomonas putida

General Information

General Information Comment Organism
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
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
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