(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Fungi: NE > Fungi incertae sedis: NE > Mucoromycota: NE > Mucoromycotina: NE > Mucoromycetes: NE > Mucorales: NE > Mucorineae: NE > Mucoraceae: NE > Mucor: NE > Mucor lusitanicus: NE > Mucor lusitanicus CBS 277.49: NE
Acidic_Lipase : muccl-a0a162riy7Mucor circinelloides f. lusitanicus CBS 277.49. AB hydrolase-1 domain-containing protein. ATG15-related-lipase : muccl-a0a168jxt4Mucor circinelloides f. lusitanicus CBS 277.49. Lipase_3 domain-containing protein, muccl-a0a168jlm0Mucor circinelloides f. lusitanicus CBS 277.49. Lipase_3 domain-containing protein. Fungal_carboxylesterase_lipase : mucc1-s2jhu5Mucor circinelloides (contaminant from bacteria?) (Mucormycosis agent) (Calyptromyces circinelloides) Uncharacterized protein. Hormone-sensitive_lipase_like : muccl-a0a168h480Mucor circinelloides f. lusitanicus CBS 277.49. Abhydrolase_3 domain-containing protein, muccl-a0a168lmw6Mucor circinelloides f. lusitanicus CBS 277.49. Abhydrolase_3 domain-containing protein, muccl-a0a168ia30Mucor circinelloides f. lusitanicus CBS 277.49. Abhydrolase_3 domain-containing protein, muccl-a0a168mc90Mucor circinelloides f. lusitanicus CBS 277.49. Lip6 Abhydrolase_3 domain-containing protein, muccl-a0a162rng6Mucor circinelloides f. lusitanicus CBS 277.49. Abhydrolase_3 domain-containing protein, muccl-a0a168hm46Mucor circinelloides f. lusitanicus CBS 277.49. Abhydrolase_3 domain-containing protein, muccl-a0a168i578Mucor circinelloides f. lusitanicus CBS 277.49. Abhydrolase_3 domain-containing protein. Lipase_3 : muccl-a0a162r071Mucor circinelloides f. lusitanicus CBS 277.49. Lipase_3 domain-containing protein, muccl-a0a168n679Mucor circinelloides f. lusitanicus CBS 277.49. Lipase_3 domain-containing protein, muccl-a0a168i244Mucor circinelloides f. lusitanicus CBS 277.49. Lipase_3 domain-containing protein, muccl-a0a168nm44Mucor circinelloides f. lusitanicus CBS 277.49. Lipase_3 domain-containing protein, muccl-a0a162mt71Mucor circinelloides f. lusitanicus CBS 277.49. Lipase_3 domain-containing protein, muccl-a0a168npk8Mucor circinelloides f. lusitanicus CBS 277.49. Lipase_3 domain-containing protein, muccl-a0a162mvq2Mucor circinelloides f. lusitanicus CBS 277.49. Lipase_3 domain-containing protein. Triacylglycerol-lipase-OBL1-like : muccl-a0a168nw20Mucor circinelloides f. lusitanicus CBS 277.49; Mucor ambiguus. Lip24 Lipase_3 domain-containing protein
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA RVSPLEFASTFEEMINYWNYDYEEHFVRTRDQYLLCLHRIKQQPVTQERT SSNASDKILKKVVLLYHGLTLTSEVWISNIEENRNLALYLTERGYDVWMG NARGNKYSQSHLTKSPKNADFWEFSINEFAMFDMPDTIDYILKKTGAPDL TYIGFSQGTAQAFGGLSINPDMNDKVNLFIAMAPAASPKGFSHPLLDGFV KAAPSIIYCLLGRKIFLKSVVFWQRIISPPIFVKLIDGAVHFLFGWHCNN MSPDQKLVSYQHLFSMTSVKSIVHWFQIISSGRFQMYDETPSLLPWSTVN TVIDHLPPKFPTKQITTPIAIFYGSGDTLVDFDILQSNLPPLSYVKSIHG WEHMDFLWAHGLEKKVYPDILKLLEHFNSPPHISHDIEEKVPLDIKYIDT ESTATVIPDNIKVSTIAVSQ
References
Title: Novel Dual-Functional Enzyme Lip10 Catalyzes Lipase and Acyltransferase Activities in the Oleaginous Fungus Mucor circinelloides Zan X, Cui F, Sun J, Zhou S, Song Y Ref: Journal of Agricultural and Food Chemistry, 67:13176, 2019 : PubMed
Lipases or triacylglycerol (TAG) lipases belong to the alpha/beta-hydrolases superfamily, which are enzymes capable of catalyzing the hydrolysis of the ester bond between fatty acids and glycerol. Interestingly, some lipases have been found to not only possess hydrolysis activity but also acyltransferase activity in yeasts and microalgae. Our present study reported a novel dual-functional Mucor circinelloides lipase Lip10 with a slight lipolysis activity but a noteworthy phospholipid/diacylglycerol acyltransferase (PDAT) activity. The purified Lip10 mutants prefer to utilize phosphatidyl serine to form TAG over phosphatidyl ethanolamine and phosphatidylcholine. Site-directed mutagenesis indicated that the histidine residue in the acyltransferase motif H-(X)4-D is indispensable for the PDAT activity of Lip10. Overexpression of the acyltransferase motif of Lip10 promoted cell growth by 12% and increased lipid production by 14% compared to the control, whilst overexpression of the lipase motif induced lipid degradation in M. circinelloides.
Lipases or triacylglycerol hydrolases are widely spread in nature and are particularly common in the microbial world. The filamentous fungus Mucor circinelloides is a potential lipase producer, as it grows well in triacylglycerol-contained culture media. So far only one lipase from M. circinelloides has been characterized, while the majority of lipases remain unknown in this fungus. In the present study, 47 potential lipase genes in M. circinelloides WJ11 and 30 potential lipase genes in M. circinelloides CBS 277.49 were identified by extensive bioinformatics analysis. An overview of these lipases is presented, including several characteristics, sub-cellular location, phylogenetic analysis and expression profiling of the lipase genes during growth and lipid accumulation. All of these proteins contained the consensus sequence for a classical lipase (GXSXG motif) and were divided into four types including alpha/beta-hydrolase_1, alpha/beta-hydrolase_3, class_3 and GDSL lipase (GDSL) based on gene annotations. Phylogenetic analyses revealed that class_3 family and alpha/beta-hydrolase_3 family were the conserved lipase family in M. circinelloides. Additionally, some lipases also contained a typical acyltransferase motif of H-(X) 4-D, and these lipases may play a dual role in lipid metabolism, catalyzing both lipid hydrolysis and transacylation reactions. The differential expression of all lipase genes were confirmed by quantitative real-time PCR, and the expression profiling were analyzed to predict the possible biological roles of these lipase genes in lipid metabolism in M. circinelloides. We preliminarily hypothesized that lipases may be involved in triacylglycerol degradation, phospholipid synthesis and beta-oxidation. Moreover, the results of sub-cellular localization, the presence of signal peptide and transcriptional analyses of lipase genes indicated that four lipase in WJ11 most likely belong to extracellular lipases with a signal peptide. These findings provide a platform for the selection of candidate lipase genes for further detailed functional study.