Cloning and Expression of a Novel Lysophospholipase Which Structurally Resembles Lecithin Cholesterol Acyltransferase

Taniyama, Yoshio; Shibata, Sachio; Kita, Satomi; Horikoshi, Kenichi; Fuse, Hiromitsu; Shirafuji, Hideo; Sumino, Yasuhiro; Fujino, Masahiko

doi:10.1006/bbrc.1999.0411

Cited by 35 publications

(31 citation statements)

References 20 publications

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“…cerevisiae. This finding coincides with previous reports of other organisms (Taniyama et al, 1999;Köffel et al, 2005;Wilson et al, 2006). In addition, we found a putative consensus motif (GNxYS) with unknown function in the TGL1-like group, which was located close to the substrate recognition site.…”

Section: T Vorapreeda and Others 1616supporting

confidence: 93%

Genome mining of fungal lipid-degrading enzymes for industrial applications

et al. 2015

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Lipases are interesting enzymes, which contribute important roles in maintaining lipid homeostasis and cellular metabolisms. Using available genome data, seven lipase families of oleaginous and non-oleaginous yeast and fungi were categorized based on the similarity of their amino acid sequences and conserved structural domains. Of them, triacylglycerol lipase (patatin-domaincontaining protein) and steryl ester hydrolase (abhydro_lipase-domain-containing protein) families were ubiquitous enzymes found in all species studied. The two essential lipases rendered signature characteristics of integral membrane proteins that might be targeted to lipid monolayer particles. At least one of the extracellular lipase families existed in each species of yeast and fungi. We found that the diversity of lipase families and the number of genes in individual families of oleaginous strains were greater than those identified in non-oleaginous species, which might play a role in nutrient acquisition from surrounding hydrophobic substrates and attribute to their obese phenotype. The gene/enzyme catalogue and relevant informative data of the lipases provided by this study are not only valuable toolboxes for investigation of the biological role of these lipases, but also convey potential in various industrial applications.

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Section: T Vorapreeda and Others 1616supporting

confidence: 93%

Genome mining of fungal lipid-degrading enzymes for industrial applications

et al. 2015

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“…6). In this study, we used the same assay conditions of lyso-PC (40 M), buffer, and ion strength under neutral conditions as reported by Taniyama et al (5). In addition, no lysophospholipase activity was found in the medium cultured with LLPL-transfected cells, in contrast with the results of Taniyama et al (5).…”

Section: Fig 4 Llpl Has Both Transacylase and Phospholipase Activitmentioning

confidence: 83%

“…Amino-terminal sequencing of the purified bovine protein yielded a sequence of GSRPPVVLVPGDM, indicating that the signal peptide cleavage site of bovine LLPL may lie between alanine 29 and glycine 30. In addition, each deduced LLPL sequence contains a putative lipase motif of AXSXG, which is also found in Bacillus lipase (5,13), and N-linked glycosylation sites, three in bovine and four in human and mouse.…”

Section: Resultsmentioning

confidence: 99%

“…These results support the conclusion that ACS is a lysosomal enzyme. Previously, Taniyama et al (5) reported that human LLPL expressed in COS-7 cells is a secreted protein that has lysophospholipase activity under neutral conditions. In this study, we failed to observe any significant increase in lysophospholipase activity in the cultured medium of COS-7 cells transfected with recombinant LLPL DNA.…”

Section: Fig 4 Llpl Has Both Transacylase and Phospholipase Activitmentioning

confidence: 99%

“…In this study, we report that a BLAST search revealed that the peptides obtained from ACS purified from bovine brain share amino acid sequences with a recently reported human gene termed lecithin:cholesterol acyltransferase (LCAT)-like lysophospholipase (LLPL) (5). To understand the biological function of ACS, the ACS gene was sequenced on the basis of its similarity to LLPL, and the gene products were characterized.…”

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confidence: 99%

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Cloning and Characterization of a Lysosomal Phospholipase A2, 1-O-Acylceramide Synthase

Hiraoka¹,

Abe²,

Shayman

2002

Journal of Biological Chemistry

107

113

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Recently, a novel enzyme, 1-O-acylceramide synthase (ACS), was purified and characterized from bovine brain. This enzyme has both calcium-independent phospholipase A 2 and transacylase activities. The discovery of this enzyme led us to propose a new pathway for ceramide metabolism in which the sn-2-acyl group of either phosphatidylethanolamine or phosphatidylcholine is transferred to the 1-hydroxyl group of ceramide. In this study, the partial amino acid sequences from the purified enzyme revealed that the enzyme contains amino acid sequences identical to those of human lecithin:cholesterol acyltransferase-like lysophospholipase (

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9 Mechanisms and mediators of neutral lipid biosynthesis in eukaryotic cells

Oelkers¹,

Sturley²

2003

Lipid Metabolism and Membrane Biogenesis

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Cloning and Expression of a Novel Lysophospholipase Which Structurally Resembles Lecithin Cholesterol Acyltransferase

Cited by 35 publications

References 20 publications

Genome mining of fungal lipid-degrading enzymes for industrial applications

Genome mining of fungal lipid-degrading enzymes for industrial applications

Cloning and Characterization of a Lysosomal Phospholipase A2, 1-O-Acylceramide Synthase

9 Mechanisms and mediators of neutral lipid biosynthesis in eukaryotic cells

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