Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.1.42 extracted from

  • Doan, T.T.; Carlsson, A.S.; Stymne, S.; Hofvander, P.
    Biochemical characteristics of AtFAR2, a fatty acid reductase from Arabidopsis thaliana that reduces fatty acyl-CoA and -ACP substrates into fatty alcohols (2016), Acta Biochim. Pol., 63, 565-570 .
    View publication on PubMed
Search for more literature for 1.2.1.42

Cloned(Commentary)

Cloned (Comment) Organism
gene FAR2, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3), transient expression of GFP-tagged FAR2 in Nicotiana benthamiana leaves under control of CaMV 35S promoter via Agrobacterium tumefaciens strain V3101::pMP90 transfection method Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00531
-
 hexadecanal pH 7.0, 30°C, recombinant enzyme Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast enzyme AtFAR2 is targeted to chloro­plasts Arabidopsis thaliana 9507
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hexadecanal + CoA + NAD+ Arabidopsis thaliana
-
 hexadecanoyl-CoA + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q08891
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hexadecanal + CoA + NAD+
-
 Arabidopsis thaliana hexadecanoyl-CoA + NADH + H+
-
 ?
additional information Arabidopsis thaliana AtFAR2 has the ability to use both, C16:0-ACP and C16:0-CoA substrates for the production of C16:0- alcohol, purified enzyme AtFAR2 is specific for acyl-ACP substrates, AtFAR2 shows the high­est activity towards C16:0-CoA, approximately 11times higher in comparison to the activity towards C18:0-CoA. AtFAR2 displays a very low activity with C18:1-CoA, and application of C14:0-CoA as a substrate generates only aldehyde and free fatty acid Arabidopsis thaliana ?
-
 ?

Synonyms

Synonyms Comment Organism
AtFAR2
-
 Arabidopsis thaliana
FAR2
-
 Arabidopsis thaliana
MS2
-
 Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 low activity with alcohols and free fatty acids occurs at above pH 9.0 Arabidopsis thaliana
6
-
 with aldehyde substrates Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
evolution AtFAR2 is highly similar in properties and substrate specificity to AtFAR6 Arabidopsis thaliana
malfunction mutations in specific genes encoding fatty acid reductases (FAR) re­sponsible for fatty alcohol production cause abnormal development of pollen. A disrupted AtFAR2 (MS2) gene in Arabidopsis thaliana results in pollen developing an abnormal exine layer and a reduced fertility pheno­type Arabidopsis thaliana
physiological function AtFAR2 is a fatty acid reductase from Arabidopsis thaliana that reduces fatty acyl-CoA and -ACP substrates into fatty alcohols, cf. EC 1.2.1.80. Enzyme AtFAR2 is the major enzyme respon­sible for exine layer functionality, AtFAR6 might provide functional redundancy to AtFAR2 Arabidopsis thaliana