Abstract
The complete gene (PG37 lip) encoding an alkaline lipase (PG37 LipI) was cloned from the genomic DNA of Penicillium cyclopium PG37. The cloned PG37 lipI is 2.020 bp in length, consisting of 632 bp of the 5′ flanking promoter region and 1.388 bp of the downstream fragment that contains 6 exons and 5 short introns. The promoter region harbors putative TATA box, CAAT box and several transcription factor binding sites. The open reading frame (ORF) encodes a PG37 LipI of 285 amino acid residues, which was predicted to contain a 20-aa signal peptide, a 7-aa propeptide and a 258-aa mature peptide with a conserved motif Gly-X-Ser-X-Gly. However, PG37 Lip shows only 32%, 30%, 28% and 26% identity with lipases of Aspergillus parasiticus, Penicillium camembertii, Thermomyces lanuginosus and Rhizomucor miehei, respectively. It was predicted that the main secondary structures of PG37 Lip are α-helix and random coil. Three amino acid residues, Ser132-Asp188-His241, compose the enzymatic active center in the tertiary structure.
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Published in Russian in Prikladnaya Biokhimiya i Mikrobiologiya, 2011, Vol. 47, No. 6, pp. 642–649.
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Zhang, H.M., Wu, M.C., Guo, J. et al. Cloning and sequence analysis of complete gene encoding an alkaline lipase from Penicillium cyclopium . Appl Biochem Microbiol 47, 586–593 (2011). https://doi.org/10.1134/S0003683811060135
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DOI: https://doi.org/10.1134/S0003683811060135