Primary structure determination of mono- and diacylglycerol lipase from Penicillium camembertii.
The complete amino acid sequence of mono- and diacylglycerol lipase from Penicillium camembertii was determined. This lipase has a single polypeptide chain consisting of 276 amino acid residues with two disulfide linkages. The primary structure was revealed by sequencing the digests of the intact and S-pyridylethylated proteins by trypsin, endoproteinase Lys-C and V8 protease. The two-dimensional electrophoresis was also carried out to confirm the internal sequence. The catalytic triad of this lipase was Ser, Asp and His, and one potential N-glycosylation site was also revealed.
Isobe
K
K
Enzyme Technology and Natural Products Chemistry Division, GBF-Gesellschaft für Biotechnologische Forschung mbH, Braunschweig, Germany.
Nokihara
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D005989:Glycerides / Q000378:metabolism; D006031:Glycosylation; D008071:Lipoprotein Lipase / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D010407:Penicillium / Q000201:enzymology*; D010446:Peptide Fragments / Q000737:chemistry; D010449:Peptide Mapping
D000596:Amino Acids; D005989:Glycerides; D010446:Peptide Fragments; D008071:Lipoprotein Lipase