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Literature summary for 2.3.1.199 extracted from

  • Ghanevati, M.; Jaworski, J.
    Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS (2002), Eur. J. Biochem., 269, 3531-3539.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Saccharomyces cerevisiae strain InvSc1 Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
C223A the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present Arabidopsis thaliana
H391A the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present Arabidopsis thaliana
H391K the mutant shows very low condensation activity Arabidopsis thaliana
H391Q the mutant shows low condensation activity (25% activity compared to the wild type enzyme) Arabidopsis thaliana
N424D the mutant shows low condensation activity Arabidopsis thaliana
N424H the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Arabidopsis thaliana 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
x * 43000, SDS-PAGE Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-PDC column chromatography Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arachidoyl-CoA + malonyl-CoA 25% activity compared to oleoyl-CoA Arabidopsis thaliana ?
-
?
additional information the enzyme shows highest activity towards saturated and monounsaturated C16 and C18. In the absence of an acyl-CoA substrate, the enzyme is unable to carry out decarboxylation of malonyl-CoA Arabidopsis thaliana ?
-
?
additional information the enzyme shows no activity with polyunsaturated linoleic acid and alpha-linolenic acid and little or no activity with acyl-CoAs having 22 carbons or longer in chain length Arabidopsis thaliana ?
-
?
oleoyl-CoA + malonyl-CoA preferred substrate Arabidopsis thaliana CoA + 3-oxo-eicosenoyl-CoA + 3-oxo-erucoyl-CoA + CO2 3-oxo-eicosenoyl-CoA is the major product ?
palmitoleoyl-CoA + malonyl-CoA
-
Arabidopsis thaliana ?
-
?
palmitoyl-CoA + malonyl-CoA
-
Arabidopsis thaliana ?
-
?
stearoyl-CoA + malonyl-CoA
-
Arabidopsis thaliana ?
-
?

Subunits

Subunits Comment Organism
? x * 43000, SDS-PAGE Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
FAE1 beta-ketoacyl-CoA synthase
-
Arabidopsis thaliana
FAE1 KCS
-
Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.6 7.5
-
Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
additional information CoA, NADPH and ATP have no effect on the condensation activity of the recombinant enzyme Arabidopsis thaliana