(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 > Dikarya: NE > Basidiomycota: NE > Agaricomycotina: NE > Agaricomycetes: NE > Agaricomycetes incertae sedis: NE > Polyporales: NE > Polyporales incertae sedis: NE > Taiwanofungus: NE > Taiwanofungus camphoratus: NE
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 MSAAHEFDEAWLAGPDGHKFYTRTYKAADVPQAVILFIHGFAEHIARYEH AHRDWADRGFTVFTYDQRGFGRTALDAEHHSKDSAYGKTRFSNQMRDIEW WTRRLKEEQSKLPLFLVGQSMGGQLALAFPTSGRKSAIKEAREHDLGSNC IQSASPCKPSLLPSYFRWVGEKAAFVLPWMPFPAEVHAENLSHDPAVNDA VSKDPLFKERGTLRGLADMLGAGEQLLWDDYRNWPKNLPVLILHGTDDKV TSCTASEEFFNKLGAEDKKLSLYPDAYHELSNEPNGVKEKFIDECISWVQ AHLPRPGDAPMSKL
Reference
Title: Characterization and heterologous expression of a novel lysophospholipase gene from Antrodia cinnamomea Hsu KH, Wang SY, Chu FH, Shaw JF Ref: J Appl Microbiol, 108:1712, 2010 : PubMed
AIMS: A novel lysophospholipase (LysoPL) from the basidiomycetous fungi Antrodia cinnamomea named ACLysoPL was cloned, heteroexpressed in Escherichia coli and characterized. METHODS AND RESULTS: The gene encoding ACLysoPL was obtained from expressed sequence tags from A. cinnamomea. The full length of this gene has a 945 -bp open reading frame encoding 314 amino acids with a molecular weight of 35.5 kDa. ACLysoPL contains a lipase consensus sequence (GXSXG) motif and a Ser-His-Asp catalytic triad. A putative peroxisomal targeting signal type 1 was found in the C-terminal. Heterologous expression of ACLysoPL in E. coli showed that the enzyme preferentially hydrolyses long-chain acyl esterases at pH 7 and 30 degrees C. ACLysoPL is a psychrophilic enzyme about 40% of whose maximum activity remained at 4 degrees C. The LysoPL activities with lysophospholipids as substrate were analysed by gas chromatography/mass spectrometry. CONCLUSION: We have identified and characterized a gene named ACLysoPL encoding a protein performing LysoPL and esterase activities. SIGNIFICANCE AND IMPACT OF THE STUDY: This is the first LysoPL of A. cinnamomea identified and characterized at the molecular level.
