The Arabidopsis acyl-CoA oxidase gene family

2000 ◽  
Vol 28 (6) ◽  
pp. 755-757 ◽  
Author(s):  
P. J. Eastmond ◽  
M. Hooks ◽  
I. A. Graham
Keyword(s):  
Fatty Acid ◽  
Full Range ◽  
Biochemical Properties ◽  
Oxidase Gene ◽  
Substrate Specificities ◽  
Fatty Acid Chain ◽  
Acyl Coa Oxidase ◽  
Chain Lengths ◽  
Peroxisomal Fatty Acid

A family of acyl-CoA oxidase isozymes catalyse the first step in the peroxisomal fatty acid β-oxidation spiral. Our group and others have recently characterized four genes from this family in the model oilseed Arabidopsis. These genes encode isozymes with different acyl-CoA substrate specificities, which together encompass the full range of fatty acid chain lengths that exist in vivo. Here we review the biochemical properties and physiological roles of the acyl-CoA oxidase isozymes.

Peroxisomal fatty acid alpha- and beta-oxidation in humans: new insights into enzymology, substrate specificities, metabolite transport and peroxisomal diseases

2001 ◽  
Vol 29 (1) ◽  
pp. A2-A2
Author(s):  
R. J. A. Wanders ◽  
S. Ferdinandusse ◽  
G. A. Jansen ◽  
E. G. van Grusven ◽  
H. R. Waterham ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Beta Oxidation ◽  
Metabolite Transport ◽  
Substrate Specificities ◽  
Peroxisomal Fatty Acid

scholarly journals Studies on the effect of an heterologous fatty acid-binding protein on acyl-CoA oxidase induction in Saccharomyces cerevisiae

1994 ◽  
Vol 301 (2) ◽  
pp. 615-620 ◽  
Author(s):  
I Smaczyńska ◽  
M Skoneczny ◽  
A Kurlandzka
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Oleic Acid ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Yeast Cells ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Acyl Coa Oxidase

The participation of fatty acid-binding protein (FABP) in the induction of peroxisomal beta-oxidation of fatty acids was investigated in vivo in an heterologous system. Bovine heart FABP was expressed in Saccharomyces cerevisiae under the control of two different promoters: a constitutive one and an oleic acid-inducible one. Constructs were introduced into yeast cells on multicopy and integrating plasmids. The heterologous FABP was present in yeast cells in two isoforms having pI values of about 5 and was able to bind oleic acid. The heterologous FABP had no significant effect on acyl-CoA oxidase activity at various concentrations of the inducing agent.

scholarly journals Overexpression of Nudt7 decreases bile acid levels and peroxisomal fatty acid oxidation in the liver

2019 ◽  
Vol 60 (5) ◽  
pp. 1005-1019 ◽  
Author(s):  
Stephanie A. Shumar ◽  
Evan W. Kerr ◽  
Paolo Fagone ◽  
Aniello M. Infante ◽  
Roberta Leonardi
Keyword(s):  
Fatty Acid ◽  
Lipid Metabolism ◽  
Bile Acid ◽  
Fatty Acid Oxidation ◽  
Acid Oxidation ◽  
Nudix Hydrolase ◽  
Peroxisomal Fatty Acid Oxidation ◽  
Chain Acyl ◽  
Peroxisomal Fatty Acid

Lipid metabolism requires CoA, an essential cofactor found in multiple subcellular compartments, including the peroxisomes. In the liver, CoA levels are dynamically adjusted between the fed and fasted states. Elevated CoA levels in the fasted state are driven by increased synthesis; however, this also correlates with decreased expression of Nudix hydrolase (Nudt)7, the major CoA-degrading enzyme in the liver. Nudt7 resides in the peroxisomes, and we overexpressed this enzyme in mouse livers to determine its effect on the size and composition of the hepatic CoA pool in the fed and fasted states. Nudt7 overexpression did not change total CoA levels, but decreased the concentration of short-chain acyl-CoAs and choloyl-CoA in fasted livers, when endogenous Nudt7 activity was lowest. The effect on these acyl-CoAs correlated with a significant decrease in the hepatic bile acid content and in the rate of peroxisomal fatty acid oxidation, as estimated by targeted and untargeted metabolomics, combined with the measurement of fatty acid oxidation in intact hepatocytes. Identification of the CoA species and metabolic pathways affected by the overexpression on Nudt7 in vivo supports the conclusion that the nutritionally driven modulation of Nudt7 activity could contribute to the regulation of the peroxisomal CoA pool and peroxisomal lipid metabolism.

Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid β-oxidation

2011 ◽  
Vol 1811 (3) ◽  
pp. 148-152 ◽  
Author(s):  
Carlo W.T. van Roermund ◽  
Wouter F. Visser ◽  
Lodewijk IJlst ◽  
Hans R. Waterham ◽  
Ronald J.A. Wanders
Keyword(s):  
Fatty Acid ◽  
Substrate Specificities ◽  
Peroxisomal Fatty Acid

scholarly journals Cyanidin-3-glucoside Lipophilic Conjugates for Topical Application: Tuning the Antimicrobial Activities with Fatty Acid Chain Length

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 340
Author(s):  
Hélder Oliveira ◽  
Patrícia Correia ◽  
Lucinda J. Bessa ◽  
Marta Guimarães ◽  
Paula Gameiro ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Fatty Acid ◽  
Antioxidant Capacity ◽  
Multidrug Resistant ◽  
Antimicrobial Activities ◽  
Aliphatic Chain ◽  
Fatty Acid Chain ◽  
The Stability ◽  
Application Tuning ◽  
Chain Lengths

Background: Natural anthocyanins present a low solubility in lipophilic media, which compromises their effective application in lipophilic systems. In this work, cyanidin-3-O-glucoside (Cy3glc) was esterified by the addition of fatty acids with increasing chain-lengths and a structure-activity relationship was performed towards the description of the best analog for skin-care applications. Methods: By enzymatic hemi-synthesis, it was possible to obtain 5 structurally related derivatives of cyanidin-3-O-glucoside with successive C2 increments in the aliphatic chain. The stability in hanks buffer and DMEM with or without FBS was followed by HPLC. The cytotoxicity against keratinocytes was evaluated by MTT assay. The antioxidant capacity was determined by using the fluorescent probe DCF-DA. The effect on enzyme activity was evaluated towards tyrosinase, collagenase, and elastase enzymes by colorimetric assays. MIC and MBC values were obtained against reference strains and against multidrug-resistant isolates. Results: In physiological conditions, cy3glc−fatty acid derivatives are more stable and may be converted to the native anthocyanin. The 5 conjugates showed lower antioxidant capacity and enzymatic inhibitory activities in comparison to the anthocyanin precursor. However, concerning the antibacterial activity, the insertion of a fatty acid chain sprouted the antibacterial activity, showing a clear biphasic effect and a more effective effect on Gram-positive bacteria. Conclusions: Cy3glc-C10 was the most effective compound considering the antimicrobial activity, although a general reduction was observed among the other activities evaluated. This work prompt further assays with a different panoply of derivatives ranging other features including saturation vs. unsaturation, even vs. odd carbon content and linear vs. branched.

scholarly journals Detection of peroxisomal fatty acyl-coenzyme A oxidase activity

1979 ◽  
Vol 182 (3) ◽  
pp. 779-788 ◽  
Author(s):  
N C Inestrosa ◽  
M Bronfman ◽  
F Leighton
Keyword(s):  
Fatty Acid ◽  
Oxidase Activity ◽  
Subcellular Fractionation ◽  
Fatty Acyl ◽  
O2 Consumption ◽  
H2o2 Generation ◽  
Acyl Coa Oxidase ◽  
Acyl Coenzyme A ◽  
Rate Limiting ◽  
Peroxisomal Fatty Acid

It has been postulated that the peroxisomal fatty acid-oxidizing system [Lazarow & de Duve (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 2043–2046; Lazarow (1978) J. Biol. Chem. 253, 1522–1528] resembles that of mitochondria, except for the first oxidative reaction. In this step, O2 would be directly reduced to H2O2 by an oxidase. Two specific procedures developed to detect the activity of the characteristic enzyme fatty acyl-CoA oxidase are presented, namely polarographic detection of palmitoyl-CoA-dependent cyanide-insensitive O2 consumption and palmitoyl-CoA-dependent H2O2 generation coupled to the peroxidation of methanol in an antimycin A-insensitive reaction. Fatty acyl-CoA oxidase activity is stimulated by FAD, which supports the flavoprotein nature postulated for this enzyme. Its activity increases 7-fold per g wet wt. of liver in rats treated with nafenopin, a hypolipidaemic drug. Subcellular fractionation of livers from normal and nafenopin-treated animals provides evidence for its peroxisomal localization. The stoicheiometry for palmitoyl-CoA-dependent O2 consumption, H2O2 generation and NAD+ reduction is 1 : 1 : 1. This suggests that fatty acyl-CoA oxidase is the rate-limiting enzyme of the peroxisomal fatty acid-oxidizing system.

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