Yamamoto S, Lampen J O
J Biol Chem. 1975 Apr 25;250(8):3212-3.
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.
地衣芽孢杆菌749/C的疏水膜青霉素酶，鉴于其在亲水性胞外酶分泌中可能发挥的作用，已得到了表征。它与胞外酶的不同之处在于，它带有一条由25个氨基酸组成的额外磷脂肽链，该链仅包含天冬氨酸、谷氨酸、甘氨酸和丝氨酸残基。其氨基末端残基是磷脂酰丝氨酸。由于这条额外的肽链可能具有相对较高的极性，磷脂基团很可能直接决定了膜酶的疏水特性。
