Properties of microsomal acyl coenzyme A reductase in mouse preputial glands

Moore, C.F.; Snyder, Fred

doi:10.1016/0003-9861(82)90052-2

Cited by 17 publications

(8 citation statements)

References 48 publications

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“…Biosynthesis of WE in other organisms involves three different enzymatic steps: acyl-CoA is reduced to fatty aldehyde that undergoes reduction to fatty alcohol followed by esterification by a fatty alcohol : acyl-CoA transacylation [14], [20], [21], [34], [35]. These reactions, first demonstrated in cell free extracts of Euglena gracilis [30] have been demonstrated in numerous organisms in both plant and animal kingdoms [14], [21], [36]–[38].…”

Section: Discussionmentioning

confidence: 99%

Wax Ester Synthesis is Required for Mycobacterium tuberculosis to Enter In Vitro Dormancy

et al. 2012

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Mycobacterium tuberculosis (Mtb) is known to produce wax esters (WE) when subjected to stress. However, nothing is known about the enzymes involved in biosynthesis of WE and their role in mycobacterial dormancy. We report that two putative Mtb fatty acyl-CoA reductase genes (fcr) expressed in E. coli display catalytic reduction of fatty acyl-CoA to fatty aldehyde and fatty alcohol. Both enzymes (FCR1/Rv3391) and FCR2/Rv1543) showed a requirement for NADPH as the reductant, a preference for oleoyl-CoA over saturated fatty acyl-CoA and were inhibited by thiol-directed reagents. We generated Mtb gene-knockout mutants for each reductase. Metabolic incorporation of 14C-oleate into fatty alcohols and WE was severely diminished in the mutants under dormancy-inducing stress conditions that are thought to be encountered by the pathogen in the host. The fatty acyl-CoA reductase activity in cell lysates of the mutants under nitric oxide stress was significantly reduced when compared with the wild type. Complementation restored the lost activity completely in the Δfcr1 mutant and partially in the Δfcr2 mutant. WE synthesis was inhibited in both Δfcr mutants. The Δfcr mutants exhibited faster growth rates, an increased uptake of 14C-glycerol suggesting increased permeability of the cell wall, increased metabolic activity levels and impaired phenotypic antibiotic tolerance under dormancy-inducing combined multiple stress conditions. Complementation of the mutants did not restore the development of antibiotic tolerance to wild-type levels. Transcript analysis of Δfcr mutants showed upregulation of genes involved in energy generation and transcription, indicating the inability of the mutants to become dormant. Our results indicate that the fcr1 and fcr2 gene products are involved in WE synthesis under in vitro dormancy-inducing conditions and that WE play a critical role in reaching a dormant state. Drugs targeted against the Mtb reductases may inhibit its ability to go into dormancy and therefore increase susceptibility of Mtb to currently used antibiotics thereby enhancing clearance of the pathogen from patients.

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Section: Discussionmentioning

confidence: 99%

Wax Ester Synthesis is Required for Mycobacterium tuberculosis to Enter In Vitro Dormancy

et al. 2012

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“…In fact, a single enzyme reaction for the fatty acid reduction appears to occur widely in nature where the FAR catalyzes reduction of fatty acylCoA to fatty alcohol directly, although aldehyde intermediates could be detected by indirect trapping assays [23]. This type of fatty acyl-CoA reductases has been identified from jojoba cotyledon, pea leaves [23,35,36] and many others [37][38][39], including the one we describe here from Euglena.…”

Section: Reconstitution Of the Euglena Wax Biosynthetic Pathway In Yeastmentioning

confidence: 97%

Fatty Acyl‐CoA Reductase and Wax Synthase from Euglena gracilis in the Biosynthesis of Medium‐Chain Wax Esters

Teerawanichpan

Qiu

2010

Lipids

105

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Euglena gracilis, a unicellular phytoflagellate, can accumulate a large amount of medium-chain wax esters under anaerobic growth conditions. Here we report the identification and characterization of two genes involved in the biosynthesis of wax esters in E. gracilis. The first gene encodes a fatty acyl-CoA reductase (EgFAR) involved in the conversion of fatty acyl-CoAs to fatty alcohols and the second gene codes for a wax synthase (EgWS) catalyzing esterification of fatty acyl-CoAs and fatty alcohols, yielding wax esters. When expressed in yeast (Saccharomyces cerevisiae), EgFAR converted myristic acid (14:0) and palmitic acid (16:0) to their corresponding alcohols (14:0Alc and 16:0Alc) with myristic acid as the preferred substrate. EgWS utilized a broad range of fatty acyl-CoAs and fatty alcohols as substrates with the preference towards myristic acid and palmitoleyl alcohol. The wax biosynthetic pathway was reconstituted by co-expressing EgFAR and EgWS in yeast. When myristic acid was fed to the yeast, myristyl myristate (14:0-14:0), myristyl palmitoleate (14:0-16:1), myristyl palmitate (14:0-16:0) and palmityl myristate (16:0-14:0) were produced. These results indicate EgFAR and EgWS are likely the two enzymes involved in the biosynthesis of medium-chain wax esters in E. gracilis.

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“…The present enzyme is similar to the fatty acid reductase from bacteria, Photobacterium phosphoream and Id'-briofischeri, in that they all use NADH as reductant to generate aldehyde [18,24]. Fatty acyl-CoA reductase from animal sources usually generate fatty alcohol with NADPH as the reductant [7,17,25].…”

Section: Resultsmentioning

confidence: 99%

“…Fatty acyl-CoA reductase that generates fatty alcohol was first demonstrated in cell free preparations from Euglena gracilis [4], and subsequently particulate preparations that catalyze fatty acyl-CoA reduction from many animal and plant tissues have been described [5][6][7][8][9]. Fatty aldehyde is used for the generation of hydrocarbons by a recently discovered biological reaction, decarbonylation [10 13].…”

Section: Introductionmentioning

confidence: 99%

Solubilization and purification of aldehyde‐generating fatty acyl‐CoA reductase from green alga Botryococcus braunii

Wang

Kolattukudy

1995

FEBS Letters

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Membrane-bound fatty acyl-CoA reductase from the green alga Botryococcus braunii has been solubilized from the microsomal preparation by 0.1% octyl ~l-ghicoside and purified to near homogeneity by Blue A agarose and palmitoyl-CoA agarose affinity column chromatography. The molecular mass of the enzyme was estimated by SDS-PAGE to be 35 kDa. The enzyme generates fatty aldehyde by reduction of fatty acyl-CoA with NADH as the reductant. The N-terminal amino acid sequence of this protein that represents the first encaryotic aldehyde-generating reductase to be purified shows high homology with the Nterminus of fatty acid reductase from bacteria.

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Properties of microsomal acyl coenzyme A reductase in mouse preputial glands

Cited by 17 publications

References 48 publications

Wax Ester Synthesis is Required for Mycobacterium tuberculosis to Enter In Vitro Dormancy

Wax Ester Synthesis is Required for Mycobacterium tuberculosis to Enter In Vitro Dormancy

Fatty Acyl‐CoA Reductase and Wax Synthase from Euglena gracilis in the Biosynthesis of Medium‐Chain Wax Esters

Solubilization and purification of aldehyde‐generating fatty acyl‐CoA reductase from green alga Botryococcus braunii

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