title: Membrane penicillinase of Bacillus licheniformis 749/C, a phospholipoprotein.
abstract: The hydrophobic membrane penicillinase of Bacillus licheniformis 749/C has been characterized in view of its possible role in secretion of the hydrophilic exoenzyme. It differs from exoenzyme in carrying an additional phospholipopeptide chain of 25 amino acids that contains only Asx, Glx, Gly, and Ser residues. The NH2-terminal residues is phosphatidylserine. since the extra peptide chain is probably relatively polar, the phospholipid group may well be directly responsible for the hydrophobic properties of the membrane enzyme.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001407:Bacillus / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D008074:Lipoproteins / Q000302:isolation & purification; D008970:Molecular Weight; D010405:Penicillinase / Q000302:isolation & purification; D010743:Phospholipids / Q000032:analysis; D011092:Polyethylene Glycols; D014462:Ultrafiltration
chemical_list: D000596:Amino Acids; D008074:Lipoproteins; D010743:Phospholipids; D011092:Polyethylene Glycols; D010405:Penicillinase