Key enzymes for biosynthesis of neutral lipid storage compounds in prokaryotes: Properties, function and occurrence of wax ester synthases/acyl-CoA:diacylglycerol acyltransferases

Wältermann, Marc; Stöveken, Tim; Steinbüchel, Alexander

doi:10.1016/j.biochi.2006.07.013

Cited by 105 publications

(115 citation statements)

References 54 publications

Supporting

Mentioning

107

Contrasting

Unclassified

Order By: Relevance

“…Several WSs have been identified in bacteria and mammals [5,15,19-21], out of which we selected five WSs for expression and characterization in S. cerevisiae CEN.PK 113-5D under control of the strong TEF1 promoter using plasmid pSP-GM2 [25]. The selected five WSs are from A. baylyi ADP1, M. hydrocarbonoclasticus DSM 8798, R. opacus PD630, Mus musculus C57BL/6 and P. arcticus 273-4.…”

Section: Resultsmentioning

confidence: 99%

“…WS from P. arcticus 273-4 has 50.4% identity to the WS from A. baylyi ADP1 [19], and has not been characterized before. In this study, its WS activity was confirmed in S. cerevisiae for the first time.…”

Section: Resultsmentioning

confidence: 99%

“…WS/DGAT from Acinetobacter baylyi ADP1 has been adopted in E. coli for ester production [4,8,16-18]. WS homologs are frequently found in the genomes of actinomycetes such as Rhodococcus [19,20] or in the genome databases of several marine bacteria like Marinobacter [19,21] and Psychrobacter [19]. Few reports are available about WS from mammals.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Functional expression and characterization of five wax ester synthases in Saccharomyces cerevisiae and their utility for biodiesel production

Shi

Valle-Rodríguez

Khoomrung

et al. 2012

Biotechnol Biofuels

View full text Add to dashboard Cite

Background Wax ester synthases (WSs) can synthesize wax esters from alcohols and fatty acyl coenzyme A thioesters. The knowledge of the preferred substrates for each WS allows the use of yeast cells for the production of wax esters that are high-value materials and can be used in a variety of industrial applications. The products of WSs include fatty acid ethyl esters, which can be directly used as biodiesel. Results Here, heterologous WSs derived from five different organisms were successfully expressed and evaluated for their substrate preference in Saccharomyces cerevisiae . We investigated the potential of the different WSs for biodiesel (that is, fatty acid ethyl esters) production in S. cerevisiae . All investigated WSs, from Acinetobacter baylyi ADP1, Marinobacter hydrocarbonoclasticus DSM 8798, Rhodococcus opacus PD630, Mus musculus C57BL/6 and Psychrobacter arcticus 273-4, have different substrate specificities, but they can all lead to the formation of biodiesel. The best biodiesel producing strain was found to be the one expressing WS from M. hydrocarbonoclasticus DSM 8798 that resulted in a biodiesel titer of 6.3 mg/L. To further enhance biodiesel production, acetyl coenzyme A carboxylase was up-regulated, which resulted in a 30% increase in biodiesel production. Conclusions Five WSs from different species were functionally expressed and their substrate preference characterized in S. cerevisiae , thus constructing cell factories for the production of specific kinds of wax ester. WS from M. hydrocarbonoclasticus showed the highest preference for ethanol compared to the other WSs, and could permit the engineered S. cerevisiae to produce biodiesel.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Functional expression and characterization of five wax ester synthases in Saccharomyces cerevisiae and their utility for biodiesel production

Shi

Valle-Rodríguez

Khoomrung

et al. 2012

Biotechnol Biofuels

View full text Add to dashboard Cite

show abstract

“…Sequence comparisons with AtfA-homologous proteins of various origins revealed that the short heptapeptide motif HHxxxDG is highly conserved in all members of this class of acyltransferases (60). An HxxxxD-like pattern represents the catalytic active-site motif as part of a conserved condensation domain (Pfam 00668) in several different nonhomologous enzyme classes.…”

Section: Atfa From a Baylyi Adp1: A Bacterial Model Enzyme For We Anmentioning

confidence: 99%

Acyltransferases in Bacteria

Röttig

Steinbüchel

2013

Microbiol Mol Biol Rev

Self Cite

148

141

View full text Add to dashboard Cite

SUMMARY Long-chain-length hydrophobic acyl residues play a vital role in a multitude of essential biological structures and processes. They build the inner hydrophobic layers of biological membranes, are converted to intracellular storage compounds, and are used to modify protein properties or function as membrane anchors, to name only a few functions. Acyl thioesters are transferred by acyltransferases or transacylases to a variety of different substrates or are polymerized to lipophilic storage compounds. Lipases represent another important enzyme class dealing with fatty acyl chains; however, they cannot be regarded as acyltransferases in the strict sense. This review provides a detailed survey of the wide spectrum of bacterial acyltransferases and compares different enzyme families in regard to their catalytic mechanisms. On the basis of their studied or assumed mechanisms, most of the acyl-transferring enzymes can be divided into two groups. The majority of enzymes discussed in this review employ a conserved acyltransferase motif with an invariant histidine residue, followed by an acidic amino acid residue, and their catalytic mechanism is characterized by a noncovalent transition state. In contrast to that, lipases rely on completely different mechanism which employs a catalytic triad and functions via the formation of covalent intermediates. This is, for example, similar to the mechanism which has been suggested for polyester synthases. Consequently, although the presented enzyme types neither share homology nor have a common three-dimensional structure, and although they deal with greatly varying molecule structures, this variety is not reflected in their mechanisms, all of which rely on a catalytically active histidine residue.

show abstract

“…The chronologically earliest reaction for acyl-neutralization of alcohols likely arose in bacteria (51), whereby long-chain alcohols or DAG are conjugated with fatty acids via the action of multifunctional WE synthases/acyl-CoA:diacylglycerol acyltransferases (WS/DGAT). TAG synthesis has also been found in prokaryotes such as Actinomyctes bacteria (2,108) and the parasite Schistosoma Mansoni (7), where it serves primarily as an energy and carbon source. These genes do not exhibit any sequence conservation to eukaryotic acyltransferases involved in TAG or WE synthesis (46, 48 -50, 100, 108).…”

Section: The Origins Of Neutral Lipidsmentioning

confidence: 99%

The genetics of neutral lipid biosynthesis: an evolutionary perspective

Turkish¹,

Sturley²

2009

American Journal of Physiology-Endocrinology and Metabolism

View full text Add to dashboard Cite

Turkish AR, Sturley SL. The genetics of neutral lipid biosynthesis: an evolutionary perspective. Am J Physiol Endocrinol Metab 297: E19 -E27, 2009. First published December 30, 2008 doi:10.1152/ajpendo.90898.2008.-The storage of fatty acids and fatty alcohols in the form of neutral lipids such as triacylglycerol (TAG), cholesteryl ester (CE), and wax ester (WE) serves to provide reservoirs for membrane formation and maintenance, lipoprotein trafficking, lipid detoxification, evaporation barriers, and fuel in times of stress or nutrient deprivation. This ancient process likely originated in actinomycetes and has persisted in eukaryotes, albeit by different molecular mechanisms. A surfeit of neutral lipids is strongly, perhaps causally, related to several human diseases such as diabetes mellitus, obesity, atherosclerosis and nonalcoholic fatty liver disease. Therefore, understanding the metabolic pathways of neutral lipid synthesis and the roles of the enzymes involved may facilitate the development of new therapeutic interventions for these syndromes. STORAGE OF FATTY ACIDS, fatty alcohols, and sterols in the form of neutral lipids serves to allocate resources for potential use in vital functions such as membrane formation, epidermal integrity, bile acid synthesis, lipoprotein trafficking, and steroidogenesis. Neutral lipids, such as cholesteryl ester (CE), triacylglycerol (TAG), and wax ester (WE), provide organisms with inert forms of energy used in conditions of nutrient deprivation and environmental stress. They also provide an excellent "sink" to buffer the toxic effects of fatty acids and fatty alcohols. In times of plenty (such as a typical Western diet), energy in the form of fat is efficiently stored, but with consequences. Elevated cytoplasmic deposition of neutral lipids (primarily CE and TAG) is a significant risk factor for several disease pathologies, including diabetes, obesity, atherosclerosis, and nonalcoholic fatty liver disease (41,53,101). For example, the accumulation of CE in smooth muscle cells and macrophages in the vessel wall comprises the earliest recognizable stage in atherosclerotic plaque formation (90). Furthermore, serum levels of TAG and total cholesterol are independent risk factors for atherosclerosis. Similarly, the loading of TAG into the cytoplasm of adipocytes represents the basic unit of obesity and thus accounts for fat accumulation in all obese syndromes.TAG, a fatty acyl ester derivative of glycerol, represents the major energy depot of all eukaryotic and some bacterial cells (16) and is formed primarily via an acyl-CoA diacylglycerol acyltransferase (DGAT) reaction, although in some organisms acyl-CoA-independent reactions also contribute to these pools. The energy of complete oxidation of the alkyl chains of TAG (38 KJ/g) is more than twice the same weight of carbohydrate or protein, and unlike polysaccharide, TAG carries no extra weight as water of solvation. Furthermore, TAG is deposited into cytoplasmic lipid droplets and thus has no effect on the osmolarity of the...

show abstract

Key enzymes for biosynthesis of neutral lipid storage compounds in prokaryotes: Properties, function and occurrence of wax ester synthases/acyl-CoA:diacylglycerol acyltransferases

Cited by 105 publications

References 54 publications

Functional expression and characterization of five wax ester synthases in Saccharomyces cerevisiae and their utility for biodiesel production

Functional expression and characterization of five wax ester synthases in Saccharomyces cerevisiae and their utility for biodiesel production

Acyltransferases in Bacteria

The genetics of neutral lipid biosynthesis: an evolutionary perspective

Contact Info

Product

Resources

About