Cloning and sequencing of the cDNA encoding lipase I from Trichosporon fermentans WU-C12.
A cDNA clone encoding extracellular lipase I (TFL I) from Trichosporon fermentans WU-C12 was isolated and characterized. The TFL I cDNA was isolated from a lambda gt10-based cDNA library using as a probe a 0.8 kb fragment, amplified by PCR with synthetic oligonucleotide corresponding to the partial amino acid sequences of TFL I. The cDNA encodes a protein consisting of 563 amino acids containing a putative signal peptide of 19 amino acids. The deduced amino acid sequence shares 99.5% overall identity with that of lipase II (GCL II) from Geotrichum candidum ATCC 34614, whereas TFL I is a trimer enzyme and GCL II monomer. Southern hybridization with the TFL I cDNA as a probe revealed that WU-C12 contained two different lipase genes.
Arai
T
T
Department of Applied Chemistry, School of Science and Engineering, Waseda University, Tokyo, Japan.
Yusa
S
S
Kirimura
K
K
Usami
S
S
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D014250:Trichosporon / Q000201:enzymology* / Q000235:genetics
D018076:DNA, Complementary; D008049:Lipase